Structural features of distinctin affecting peptide biological and biochemical properties (513 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.379, 5-year impact factor: 3.402
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-48249129108&partnerID=40&md5=3140342195fa61c0acb14ad164aba6dc
Keywords: Chains, Dyes, Experiments, Health, Lipid Bilayers, Polypeptides, American Chemical Society (acs), Anti Microbial Activities, Antimicrobial Peptide (amp), Aqueous Medium, Bactericidal Properties, Biochemical Properties, Disulfide Bonds, Disulfide Bridges, Membrane Surfaces, Microbial Membranes, Peptide Chains, Permeabilization, Quaternary Structures, Secondary Structures, Structural Features, Amines, Distinctin, Homodimer, Liposome, Monomer, Polypeptide Antibiotic Agent, Proteinase, Antimicrobial Activity, Aqueous Solution, Article, Bactericidal Activity, Biochemical Composition, Cell Permeabilization, Comparative Study, Controlled Study, Enzyme Mechanism, Human, Human Cell, Molecule, Peptide Analysis, Peptide Synthesis, Priority Journal, Protein Quaternary Structure, Protein Secondary Structure, Structure Activity Relation, Supramolecular Chemistry, Amino Acid Sequence, Anti-Bacterial Agents, Cell Membrane Permeability, Chromatography, Computer Simulation, Dimerization, Magnetic Resonance Spectroscopy, Microbial Sensitivity Tests, Models, Biological, Molecular Sequence Data, Spectrometry, Matrix-Assisted Laser Desorption-Ionization, Fourier Transform Infrared, Structure-Activity Relationship,
Affiliations:
*** IBB - CNR ***
Bruno Kessler Foundation, Institute of Biophysics, National Research Council, 38100 Povo (Trento), Italy
Institute of Infectious Diseases and Public Health, Polytechnic Marche University, 60200 Ancona, Italy
Institute of Biomolecular Chemistry, National Research Council, 80078 Pozzuoli (Naples), Italy
Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, 80147 Naples, Italy
Laboratory of Bioorganic Chemistry, Department of Physics, University of Trento, 38100 Povo (Trento), Italy
Inbios S.r.l., 80078 Pozzuoli (Naples), Italy
Institute of Biostructures and Bioimages, National Research Council, 80138 Naples, Italy
Inbios S. r. l., 80078 Pozzuoli (Naples), Italy
References:
Barra, D., Simmaco, M., Amphibian skin: A promising resource for antimicrobial peptides (1995) Trends Biotechnol, 13, pp. 205-20
Zasloff, M., Antimicrobial peptides of multicellular organisms (2002) Nature, 415, pp. 389-395
Yeaman, M.R., Yount, N.Y., Mechanisms of antimicrobial peptide action and resistence (2003) Pharmacol. Rev, 55, pp. 27-55
Oren, Z., Shai, Y., Mode of action of linear amphipathic α-helical antimicrobial peptides (1999) Biopolymers, 47, pp. 451-463
Lequin, O., Ladram, A., Chabbert, L., Bruston, F., Convert, O., Vanhoye, D., Chassaing, G., Amiche, M., Dermaseptin S9, an α-helical antimicrobial peptide with a hydrophobic core and cationic termini (2006) Biochemistry, 45, pp. 468-480
Vignal, E., Chavanieu, A., Roch, P., Chiche, L., Grassy, G., Calas, B., Aumelas, A., Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles (1998) Eur. J. Biochem, 253, pp. 221-228
Bechinger, B., Zasloff, M., Opella, S.J., Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy (1998) Biophys. J, 74, pp. 981-987
Park, S.H., Kim, Y.K., Park, J.W., Lee, B., Lee, B.J., Solution structure of the antimicrobial peptide gaegurin 4 by 1H and 15N NMR spectroscopy (2000) Eur. J. Biochem, 267, pp. 2695-2704
Batista, C.V., Scaloni, A., Rigden, D.J., Silva, L.R., Rodrigues Romero, A., Dukor, R., Sebben, A., Bloch, C., A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta (2001) FEBS Lett, 494, pp. 85-89
Lee, I.H., Lee, Y.S., Kim, C.H., Kim, C.R., Hong, T., Menzel, L., Boo, L.M., Lehrer, R.I., Dicynthaurin: An antimicrobial peptide from hemocytes of the solitary tunicate Halocynthia aurantium (2001) Biochim. Biophys. Acta, 1527, pp. 141-148
Jang, W.S., Kim, K.N., Lee, Y.S., Nam, M.H., Lee, I.H., Halocidin: A new antimicrobial peptide from hemocytes of the solitary tunicate Halocynthia aurantium (2002) FEBS Lett, 521, pp. 81-86
Yomogida, S., Nagaoka, I., Yamashita, T., Purification of the 11- and 5-kDa antibacterial polypeptides from guinea pig neutrophils (1996) Arch. Biochem. Biophys, 328, pp. 219-226
Scocchi, M., Zelezetsky, I., Benincasa, M., Gennaro, R., Mazzoli, A., Tossi, A., Structural aspects and biological properties of the cathelicidin PMAP-36 (2005) FEBS J, 272, pp. 4398-4406
Jang, W.S., Kim, C.H., Kim, K.N., Park, S.Y., Lee, J.H., Son, S.M., Lee, I.H., Biological activities of synthetic analogs of halocidin, an antimicrobial peptide from the tunicate Halocynthia aurantium (2003) Antimicrob. Agents Chemother, 47, pp. 2481-2486
Okuda, D., Yomogida, S., Tamura, H., Nagaoka, I., Determination of the antibacterial and lipopolysaccharide-neutralizing regions of guinea pig neutrophil cathelicidin peptide CAP11 (2006) Antimicrob. Agents Chemother, 50, pp. 2602-2607
Raimondo, D., Andreotti, G., Saint, N., Amodeo, P., Renzone, G., Sanseverino, M., Zocchi, I., Scaloni, A., A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin (2005) Proc. Natl. Acad. Sci. U.S.A, 102, pp. 6309-6314
Mangoni, M.L., Saugar, J.M., Dellisanti, M., Barra, D., Simmaco, M., Rivas, L., Temporins, small antimicrobial peptides with leishmanicidal activity (2005) J. Biol. Chem, 280, pp. 984-990
Brand, G.D., Leite, J.R., Silva, L.P., Albuquerque, S., Prates, M.V., Azevedo, R.B., Carregaro, V., Bloch, C., Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells (2002) J. Biol. Chem, 277, pp. 49332-49340
Ohsaki, Y., Gazdar, A.F., Chen, H.C., Johnson, B.E., Antitumor activity of magainin analogues against human lung cancer cell lines (1992) Cancer Res, 52, pp. 3534-3538
Cruciani, R.A., Barker, J.L., Zasloff, M., Chen, H.C., Colamonici, O., Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation (1991) Proc. Natl. Acad. Sci. U.S.A, 88, pp. 3792-3796
Zairi, A., Serres, C., Tangy, F., Jouannet, P., Hani, K., In vitro spermicidal activity of peptides from amphibian skin: Dermaseptin S4 and derivatives (2008) Bioorg. Med. Chem, 16, pp. 266-275
Shai, Y., Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides (1999) Biochim. Biophys. Acta, 1462, pp. 55-70
Matsuzaki, K., Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes (1999) Biochim. Biophys. Acta, 1462, pp. 1-10
Yang, L., Weiss, T.M., Lehrer, R.I., Huang, H.W., Crystallization of antimicrobial pores in membranes: Magainin and protegrin (2000) Biophys. J, 79, pp. 2002-2009
(2003) Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically, Approved Standard M7-A6, , Clinical and Laboratory Standards Institute , Villanova, PA
Scaloni, A., Dalla Serra, M., Amodeo, P., Mannina, L., Vitale, R.M., Segre, A.L., Cruciani, O., Fogliano, V., Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: Cormycin A (2004) Biochem. J, 384, pp. 25-36
Coraiola, M., Lo Cantore, P., Lazzaroni, S., Evidente, A., Iacobellis, N.S., Dalla Serra, M., WLIP and tolaasin I, lipodepsipeptides from Pseudomonas reactans and Pseudomonas tolaasii, permeabilise model membranes (2006) Biochim. Biophys. Acta, 1758, pp. 1713-1722
Alvarez, C., Dalla Serra, M., Potrich, C., Bernhart, I., Tejuca, M., Martinez, D., Pazos, I.F., Menestrina, G., Effects of lipid composition on membrane permeabilization by Sticholysin I and II, two cytolysins of the sea anemone Stichodactyia helianthus (2001) Biophys. J, 80, pp. 2761-2774
Menestrina, G., Use of Fourier-transformed infrared spectroscopy (FTIR) for secondary structure determination of staphylococcal pore-forming toxins (2000) Bacterial toxins, methods and protocols, pp. 115-132. , Holst, O, Ed, pp, Humana Press, Totowa, NJ
Goormaghtigh, E., Raussens, V., Ruysschaert, J.M., Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes (1999) Biochim. Biophys. Acta, 1422, pp. 105-185
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Gordon, L.M., Mobley, P.W., Pilpa, R., Sherman, M.A., Waring, A.J., Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using 13C-enhanced Fourier transform IR spectroscopy (2002) Biochim. Biophys. Acta, 1559, pp. 96-120
Fontana, A., Polverino de Laureto, P., De Filippis, V., Scaramella, E., Zambonin, M., (1997) Folding Des, 2, pp. R17-R26
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Huang, H.W., Molecular mechanism of antimicrobial peptides: The origin of cooperativity (2006) Biochim. Biophys. Acta, 1758, pp. 1292-1302
Liu, F., Lewis, R.N.A.H., Hodges, R.S., McElhaney, R.N., A differential scanning calorimetric and 31P NMR spectroscopic study of the effect of transmembrane α-helical peptides on the lamellar-reversed hexagonal phase transition of phosphatidylethanolamine model membranes (2001) Biochemistry, 40, pp. 760-768
Hori, Y., Demura, M., Niidome, T., Aoyagi, H., Asakura, T., Orientational behavior of phospholipid membranes with mastoparan studied by 31P solid state NMR (1999) FEBS Lett, 455, pp. 228-232
Dennis, E.A., Plueckthun, A., 31P NMR of phospholipids in micelles (1984) 31P NMR, Principles and Applications, pp. 423-446. , Gorenstein, D. G, Ed, pp, Academic Press, New York
Anderluh, G., Dalla Serra, M., Viero, G., Guella, G., Macek, P., Menestrina, G., Pore formation by equinatoxin II, an eukaryotic protein toxin, occurs by induction of non-lamellar lipid structures (2003) J. Biol. Chem, 278, pp. 45216-45223
Banerjee, U., Zidovetzki, R., Birge, R.R., Chan, S.I., Interaction of alamethicin with lecithin bilayers: A 31P and 2H NMR study (1985) Biochemistry, 24, pp. 7621-7627
Bechinger, B., Skladnev, D.A., Ogrel, A., Li, X., Rogozhkina, E.V., Ovchinnikova, T.V., O'Neil, J.D., Raap, J., 15N and 31P solid-state NMR investigations on the orientation of zervamicin II and alamethicin in phosphatidylcholine membranes (2001) Biochemistry, 40, pp. 9428-9437
Loll, P.J., Miller, R., Weeks, C.M., Axelsen, P.H., A ligand-mediated dimerization mode for vancomycin (1998) Chem. Biol, 5, pp. 293-298
Hornef, M.W., Pütsep, K., Karlsson, J., Refai, E., Andersson, M., Increased diversity of intestinal antimicrobial peptides by covalent dimer formation (2004) Nat. Immunol, 5, pp. 836-843
Oren, Z., Lerman, J.C., Gudmundsson, G.H., Agerberth, B., Shai, Y., Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity (1999) Biochem. J, 341, pp. 501-513
Schibli, D.J., Hunter, H.N., Aseyev, V., Starner, T.D., Wiencek Jr., J.M., Tack, B.F., Vogel, H.J., The solution structures of the human β-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus (2002) J. Biol. Chem, 277, pp. 8279-8289
Dempsey, C.E., Ueno, S., Avison, M.B., Enhanced membrane permeabilization and antibacterial activity of a disulfide-dimerized magainin analogue (2003) Biochemistry, 42, pp. 402-409
Tencza, S.B., Creighton, D.J., Yuan, T., Vogel, H.J., Montelaro, R.C., Mietzner, T.A., Lentivirus-derived antimicrobial peptides: Increased potency by sequence engineering and dimerization (1999) J. Antimicrob. Chemother, 44, pp. 33-41
Yang, L., Harroun, T.A., Weiss, T.M., Ding, L., Huang, H.W., Barrel-stave model or toroidal model? A case study on melittin pores (2001) Biophys. J, 81, pp. 1475-1485
Lee, M.T., Chen, F.Y., Huang, H.W., Energetics of pore formation induced by membrane active peptides (2004) Biochemistry, 43, pp. 3590-3599
Glaser, R.W., Sachse, C., Dürr, U.H., Wadhwani, P., Ulrich, A.S., Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels (2004) J. Magn. Reson, 168, pp. 153-163
Tremouilhac, P., Strandberg, E., Wadhwani, P., Ulrich, A.S., Conditions affecting the re-alignment of the antimicrobial peptide PGLa in membranes as monitored by solid state 2H-NMR (2006) Biochim. Biophys. Acta, 1758, pp. 1330-1342
Giacometti, A., Cirioni, O., Ghiselli, R., Orlando, F., Silvestri, C., Renzone, G., Testa, I., Scalise, G., Distinctin improves the efficacies of glycopeptides and betalactams against staphylococcal Biofilm in an experimental model of central venous catheter infection (2007) J. Biomed. Mater. Res., Part A, 81, pp. 233-239
Yeaman, M. R., Yount, N. Y., Mechanisms of antimicrobial peptide action and resistence (2003) Pharmacol. Rev, 55, pp. 27-55
Park, S. H., Kim, Y. K., Park, J. W., Lee, B., Lee, B. J., Solution structure of the antimicrobial peptide gaegurin 4 by 1H and 15N NMR spectroscopy (2000) Eur. J. Biochem, 267, pp. 2695-2704
Batista, C. V., Scaloni, A., Rigden, D. J., Silva, L. R., Rodrigues Romero, A., Dukor, R., Sebben, A., Bloch, C., A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta (2001) FEBS Lett, 494, pp. 85-89
Lee, I. H., Lee, Y. S., Kim, C. H., Kim, C. R., Hong, T., Menzel, L., Boo, L. M., Lehrer, R. I., Dicynthaurin: An antimicrobial peptide from hemocytes of the solitary tunicate Halocynthia aurantium (2001) Biochim. Biophys. Acta, 1527, pp. 141-148
Jang, W. S., Kim, K. N., Lee, Y. S., Nam, M. H., Lee, I. H., Halocidin: A new antimicrobial peptide from hemocytes of the solitary tunicate Halocynthia aurantium (2002) FEBS Lett, 521, pp. 81-86
Jang, W. S., Kim, C. H., Kim, K. N., Park, S. Y., Lee, J. H., Son, S. M., Lee, I. H., Biological activities of synthetic analogs of halocidin, an antimicrobial peptide from the tunicate Halocynthia aurantium (2003) Antimicrob. Agents Chemother, 47, pp. 2481-2486
Mangoni, M. L., Saugar, J. M., Dellisanti, M., Barra, D., Simmaco, M., Rivas, L., Temporins, small antimicrobial peptides with leishmanicidal activity (2005) J. Biol. Chem, 280, pp. 984-990
Brand, G. D., Leite, J. R., Silva, L. P., Albuquerque, S., Prates, M. V., Azevedo, R. B., Carregaro, V., Bloch, C., Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells (2002) J. Biol. Chem, 277, pp. 49332-49340
Cruciani, R. A., Barker, J. L., Zasloff, M., Chen, H. C., Colamonici, O., Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation (1991) Proc. Natl. Acad. Sci. U. S. A, 88, pp. 3792-3796
(2003) Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically, Approved Standard M7-A6, , Clinical and Laboratory Standards Institute, Villanova, PA
Gordon, L. M., Mobley, P. W., Pilpa, R., Sherman, M. A., Waring, A. J., Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using 13C-enhanced Fourier transform IR spectroscopy (2002) Biochim. Biophys. Acta, 1559, pp. 96-120
Huang, H. W., Molecular mechanism of antimicrobial peptides: The origin of cooperativity (2006) Biochim. Biophys. Acta, 1758, pp. 1292-1302
Liu, F., Lewis, R. N. A. H., Hodges, R. S., McElhaney, R. N., A differential scanning calorimetric and 31P NMR spectroscopic study of the effect of transmembrane -helical peptides on the lamellar-reversed hexagonal phase transition of phosphatidylethanolamine model membranes (2001) Biochemistry, 40, pp. 760-768
Dennis, E. A., Plueckthun, A., 31P NMR of phospholipids in micelles (1984) 31P NMR, Principles and Applications, pp. 423-446. , Gorenstein, D. G, Ed, pp, Academic Press, New York
Loll, P. J., Miller, R., Weeks, C. M., Axelsen, P. H., A ligand-mediated dimerization mode for vancomycin (1998) Chem. Biol, 5, pp. 293-298
Hornef, M. W., P tsep, K., Karlsson, J., Refai, E., Andersson, M., Increased diversity of intestinal antimicrobial peptides by covalent dimer formation (2004) Nat. Immunol, 5, pp. 836-843
Schibli, D. J., Hunter, H. N., Aseyev, V., Starner, T. D., Wiencek Jr., J. M., Tack, B. F., Vogel, H. J., The solution structures of the human -defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus (2002) J. Biol. Chem, 277, pp. 8279-8289
Dempsey, C. E., Ueno, S., Avison, M. B., Enhanced membrane permeabilization and antibacterial activity of a disulfide-dimerized magainin analogue (2003) Biochemistry, 42, pp. 402-409
Tencza, S. B., Creighton, D. J., Yuan, T., Vogel, H. J., Montelaro, R. C., Mietzner, T. A., Lentivirus-derived antimicrobial peptides: Increased potency by sequence engineering and dimerization (1999) J. Antimicrob. Chemother, 44, pp. 33-41
Lee, M. T., Chen, F. Y., Huang, H. W., Energetics of pore formation induced by membrane active peptides (2004) Biochemistry, 43, pp. 3590-3599
Glaser, R. W., Sachse, C., D rr, U. H., Wadhwani, P., Ulrich, A. S., Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels (2004) J. Magn. Reson, 168, pp. 153-163
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.379, 5-year impact factor: 3.402
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-48249129108&partnerID=40&md5=3140342195fa61c0acb14ad164aba6dc
Keywords: Chains, Dyes, Experiments, Health, Lipid Bilayers, Polypeptides, American Chemical Society (acs), Anti Microbial Activities, Antimicrobial Peptide (amp), Aqueous Medium, Bactericidal Properties, Biochemical Properties, Disulfide Bonds, Disulfide Bridges, Membrane Surfaces, Microbial Membranes, Peptide Chains, Permeabilization, Quaternary Structures, Secondary Structures, Structural Features, Amines, Distinctin, Homodimer, Liposome, Monomer, Polypeptide Antibiotic Agent, Proteinase, Antimicrobial Activity, Aqueous Solution, Article, Bactericidal Activity, Biochemical Composition, Cell Permeabilization, Comparative Study, Controlled Study, Enzyme Mechanism, Human, Human Cell, Molecule, Peptide Analysis, Peptide Synthesis, Priority Journal, Protein Quaternary Structure, Protein Secondary Structure, Structure Activity Relation, Supramolecular Chemistry, Amino Acid Sequence, Anti-Bacterial Agents, Cell Membrane Permeability, Chromatography, Computer Simulation, Dimerization, Magnetic Resonance Spectroscopy, Microbial Sensitivity Tests, Models, Biological, Molecular Sequence Data, Spectrometry, Matrix-Assisted Laser Desorption-Ionization, Fourier Transform Infrared, Structure-Activity Relationship,
Affiliations:
*** IBB - CNR ***
Bruno Kessler Foundation, Institute of Biophysics, National Research Council, 38100 Povo (Trento), Italy
Institute of Infectious Diseases and Public Health, Polytechnic Marche University, 60200 Ancona, Italy
Institute of Biomolecular Chemistry, National Research Council, 80078 Pozzuoli (Naples), Italy
Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, 80147 Naples, Italy
Laboratory of Bioorganic Chemistry, Department of Physics, University of Trento, 38100 Povo (Trento), Italy
Inbios S.r.l., 80078 Pozzuoli (Naples), Italy
Institute of Biostructures and Bioimages, National Research Council, 80138 Naples, Italy
Inbios S. r. l., 80078 Pozzuoli (Naples), Italy
References:
Barra, D., Simmaco, M., Amphibian skin: A promising resource for antimicrobial peptides (1995) Trends Biotechnol, 13, pp. 205-20
Zasloff, M., Antimicrobial peptides of multicellular organisms (2002) Nature, 415, pp. 389-395
Yeaman, M.R., Yount, N.Y., Mechanisms of antimicrobial peptide action and resistence (2003) Pharmacol. Rev, 55, pp. 27-55
Oren, Z., Shai, Y., Mode of action of linear amphipathic α-helical antimicrobial peptides (1999) Biopolymers, 47, pp. 451-463
Lequin, O., Ladram, A., Chabbert, L., Bruston, F., Convert, O., Vanhoye, D., Chassaing, G., Amiche, M., Dermaseptin S9, an α-helical antimicrobial peptide with a hydrophobic core and cationic termini (2006) Biochemistry, 45, pp. 468-480
Vignal, E., Chavanieu, A., Roch, P., Chiche, L., Grassy, G., Calas, B., Aumelas, A., Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles (1998) Eur. J. Biochem, 253, pp. 221-228
Bechinger, B., Zasloff, M., Opella, S.J., Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy (1998) Biophys. J, 74, pp. 981-987
Park, S.H., Kim, Y.K., Park, J.W., Lee, B., Lee, B.J., Solution structure of the antimicrobial peptide gaegurin 4 by 1H and 15N NMR spectroscopy (2000) Eur. J. Biochem, 267, pp. 2695-2704
Batista, C.V., Scaloni, A., Rigden, D.J., Silva, L.R., Rodrigues Romero, A., Dukor, R., Sebben, A., Bloch, C., A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta (2001) FEBS Lett, 494, pp. 85-89
Lee, I.H., Lee, Y.S., Kim, C.H., Kim, C.R., Hong, T., Menzel, L., Boo, L.M., Lehrer, R.I., Dicynthaurin: An antimicrobial peptide from hemocytes of the solitary tunicate Halocynthia aurantium (2001) Biochim. Biophys. Acta, 1527, pp. 141-148
Jang, W.S., Kim, K.N., Lee, Y.S., Nam, M.H., Lee, I.H., Halocidin: A new antimicrobial peptide from hemocytes of the solitary tunicate Halocynthia aurantium (2002) FEBS Lett, 521, pp. 81-86
Yomogida, S., Nagaoka, I., Yamashita, T., Purification of the 11- and 5-kDa antibacterial polypeptides from guinea pig neutrophils (1996) Arch. Biochem. Biophys, 328, pp. 219-226
Scocchi, M., Zelezetsky, I., Benincasa, M., Gennaro, R., Mazzoli, A., Tossi, A., Structural aspects and biological properties of the cathelicidin PMAP-36 (2005) FEBS J, 272, pp. 4398-4406
Jang, W.S., Kim, C.H., Kim, K.N., Park, S.Y., Lee, J.H., Son, S.M., Lee, I.H., Biological activities of synthetic analogs of halocidin, an antimicrobial peptide from the tunicate Halocynthia aurantium (2003) Antimicrob. Agents Chemother, 47, pp. 2481-2486
Okuda, D., Yomogida, S., Tamura, H., Nagaoka, I., Determination of the antibacterial and lipopolysaccharide-neutralizing regions of guinea pig neutrophil cathelicidin peptide CAP11 (2006) Antimicrob. Agents Chemother, 50, pp. 2602-2607
Raimondo, D., Andreotti, G., Saint, N., Amodeo, P., Renzone, G., Sanseverino, M., Zocchi, I., Scaloni, A., A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin (2005) Proc. Natl. Acad. Sci. U.S.A, 102, pp. 6309-6314
Mangoni, M.L., Saugar, J.M., Dellisanti, M., Barra, D., Simmaco, M., Rivas, L., Temporins, small antimicrobial peptides with leishmanicidal activity (2005) J. Biol. Chem, 280, pp. 984-990
Brand, G.D., Leite, J.R., Silva, L.P., Albuquerque, S., Prates, M.V., Azevedo, R.B., Carregaro, V., Bloch, C., Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells (2002) J. Biol. Chem, 277, pp. 49332-49340
Ohsaki, Y., Gazdar, A.F., Chen, H.C., Johnson, B.E., Antitumor activity of magainin analogues against human lung cancer cell lines (1992) Cancer Res, 52, pp. 3534-3538
Cruciani, R.A., Barker, J.L., Zasloff, M., Chen, H.C., Colamonici, O., Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation (1991) Proc. Natl. Acad. Sci. U.S.A, 88, pp. 3792-3796
Zairi, A., Serres, C., Tangy, F., Jouannet, P., Hani, K., In vitro spermicidal activity of peptides from amphibian skin: Dermaseptin S4 and derivatives (2008) Bioorg. Med. Chem, 16, pp. 266-275
Shai, Y., Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides (1999) Biochim. Biophys. Acta, 1462, pp. 55-70
Matsuzaki, K., Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes (1999) Biochim. Biophys. Acta, 1462, pp. 1-10
Yang, L., Weiss, T.M., Lehrer, R.I., Huang, H.W., Crystallization of antimicrobial pores in membranes: Magainin and protegrin (2000) Biophys. J, 79, pp. 2002-2009
(2003) Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically, Approved Standard M7-A6, , Clinical and Laboratory Standards Institute , Villanova, PA
Scaloni, A., Dalla Serra, M., Amodeo, P., Mannina, L., Vitale, R.M., Segre, A.L., Cruciani, O., Fogliano, V., Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: Cormycin A (2004) Biochem. J, 384, pp. 25-36
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(2003) Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically, Approved Standard M7-A6, , Clinical and Laboratory Standards Institute, Villanova, PA
Gordon, L. M., Mobley, P. W., Pilpa, R., Sherman, M. A., Waring, A. J., Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using 13C-enhanced Fourier transform IR spectroscopy (2002) Biochim. Biophys. Acta, 1559, pp. 96-120
Huang, H. W., Molecular mechanism of antimicrobial peptides: The origin of cooperativity (2006) Biochim. Biophys. Acta, 1758, pp. 1292-1302
Liu, F., Lewis, R. N. A. H., Hodges, R. S., McElhaney, R. N., A differential scanning calorimetric and 31P NMR spectroscopic study of the effect of transmembrane -helical peptides on the lamellar-reversed hexagonal phase transition of phosphatidylethanolamine model membranes (2001) Biochemistry, 40, pp. 760-768
Dennis, E. A., Plueckthun, A., 31P NMR of phospholipids in micelles (1984) 31P NMR, Principles and Applications, pp. 423-446. , Gorenstein, D. G, Ed, pp, Academic Press, New York
Loll, P. J., Miller, R., Weeks, C. M., Axelsen, P. H., A ligand-mediated dimerization mode for vancomycin (1998) Chem. Biol, 5, pp. 293-298
Hornef, M. W., P tsep, K., Karlsson, J., Refai, E., Andersson, M., Increased diversity of intestinal antimicrobial peptides by covalent dimer formation (2004) Nat. Immunol, 5, pp. 836-843
Schibli, D. J., Hunter, H. N., Aseyev, V., Starner, T. D., Wiencek Jr., J. M., Tack, B. F., Vogel, H. J., The solution structures of the human -defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus (2002) J. Biol. Chem, 277, pp. 8279-8289
Dempsey, C. E., Ueno, S., Avison, M. B., Enhanced membrane permeabilization and antibacterial activity of a disulfide-dimerized magainin analogue (2003) Biochemistry, 42, pp. 402-409
Tencza, S. B., Creighton, D. J., Yuan, T., Vogel, H. J., Montelaro, R. C., Mietzner, T. A., Lentivirus-derived antimicrobial peptides: Increased potency by sequence engineering and dimerization (1999) J. Antimicrob. Chemother, 44, pp. 33-41
Lee, M. T., Chen, F. Y., Huang, H. W., Energetics of pore formation induced by membrane active peptides (2004) Biochemistry, 43, pp. 3590-3599
Glaser, R. W., Sachse, C., D rr, U. H., Wadhwani, P., Ulrich, A. S., Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels (2004) J. Magn. Reson, 168, pp. 153-163
Structural features of distinctin affecting peptide biological and biochemical properties
The antimicrobial peptide distinctin consists of two peptide chains linked by a disulfide bridge; it presents a peculiar fold in water resulting from noncovalent dimerization of two heterodimeric molecules. To investigate the contribution of each peptide chain and the S-S bond to distinctin biochemical properties, different monomeric and homodimeric peptide analogues were synthesized and comparatively evaluated with respect to the native molecule. Our experiments demonstrate that the simultaneous occurrence of both peptide chains and the disulfide bond is essential for the formation of the quaternary structure of distinctin in aqueous media, able to resist protease action. In contrast, distinctin and monomeric and homodimeric analogues exhibited comparable antimicrobial activities, suggesting only a partial contribution of the S-S bond to peptide killing effectiveness. Relative bactericidal properties paralleled liposome permeabilization results, definitively demonstrating that microbial membranes are the main target of distinctin activity. Various biophysical experiments performed in membrane-mimicking media, before and after peptide addition, provided information about peptide secondary structure, lipid bilayer organization, and lipid-peptide orientation with respect to membrane surface. These data were instrumental in the generation of putative models of peptide-lipid supramolecular pore complexes.
The antimicrobial peptide distinctin consists of two peptide chains linked by a disulfide bridge; it presents a peculiar fold in water resulting from noncovalent dimerization of two heterodimeric molecules. To investigate the contribution of each peptide chain and the S-S bond to distinctin biochemical properties, different monomeric and homodimeric peptide analogues were synthesized and comparatively evaluated with respect to the native molecule. Our experiments demonstrate that the simultaneous occurrence of both peptide chains and the disulfide bond is essential for the formation of the quaternary structure of distinctin in aqueous media, able to resist protease action. In contrast, distinctin and monomeric and homodimeric analogues exhibited comparable antimicrobial activities, suggesting only a partial contribution of the S-S bond to peptide killing effectiveness. Relative bactericidal properties paralleled liposome permeabilization results, definitively demonstrating that microbial membranes are the main target of distinctin activity. Various biophysical experiments performed in membrane-mimicking media, before and after peptide addition, provided information about peptide secondary structure, lipid bilayer organization, and lipid-peptide orientation with respect to membrane surface. These data were instrumental in the generation of putative models of peptide-lipid supramolecular pore complexes.
Structural features of distinctin affecting peptide biological and biochemical properties
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Structural features of distinctin affecting peptide biological and biochemical properties
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Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 527-534.
Impact Factor: 2.863
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Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (544 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
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Bonomo RP, Bruno V, Conte E, De Guidi G, La Mendola D, Maccarrone G, Nicoletti F, Rizzarelli E, Sortino S, Vecchio G
* Potentiometric, spectroscopic and antioxidant activity studies of SOD mimics containing carnosine (385 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2003; (23): 4406-4415.
Impact Factor: 2.908
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Improta R, Mele F, Crescenzi O, Benzi C, Barone V
* Understanding the role of stereoelectronic effects in determining collagen stability. 2. A quantum mechanical/molecular mechanical study of (Proline-Proline-Glycine)n polypeptides (340 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2002 Jul 3; 124(26): 7857-7865.
Impact Factor: 6.201
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Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
* Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95 (384 views)
J Cryst Growth (ISSN: 0022-0248), 2001; 232(1-4): 481-488.
Impact Factor: 1.283
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
Crystal Structure Of A Collagen-Like Polypeptide With Repeating Sequence Pro-Hyp-Gly At 1. 4 Ang Resolution: Implications For Collagen Hydration (436 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 8-13.
Impact Factor: 2.405
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D'Andrea LD, Mazzeo M, Isernia C, Rossi F, Saviano M, Gallo P, Paolillo L, Pedone C
Solution conformational preferences of a peptidic analogue of a natural macrolide (381 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(3): 349-361.
Impact Factor: 2.425
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Zanotti G, Maione A, Rossi F, Saviano M, Pedone C, Tancredi T
BIOACTIVE PEPTIDES - CONFORMATIONAL STUDY OF A CYSTINYL CYCLOHEPTAPEPTIDE IN ITS FREE AND CALCIUM COMPLEXED FORMS (581 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1993 Jul; 33(7): 1083-1091.
Impact Factor: 2.425
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Di Blasio B, Lombardi A, D'Auria G, Saviano M, Isernia C, Maglio O, Paolillo L, Pedone C, Pavone V
Beta-Alanine Containing Peptides: Gamma-Turns In Cyclotetrapeptides (560 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1993 Apr; 31(10): 621-631.
Impact Factor: 2.425
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Pavone V, Lombardi A, D'Auria G, Saviano M, Nastri F, Paolillo L, Di Blasio B, Pedone C
β-Alanine containing peptides: A novel molecular tool for the design of γ-turns (813 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1992 Feb; 32(2): 173-184.
Impact Factor: 2.425
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Tancredi T, Benedetti E, Grimaldi M, Pedone C, Rossi F, Saviano M, Temussi PA, Zanotti G
Ion binding of cyclolinopeptide A: An NMR and CD conformational study (633 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1991 May; 31(6): 761-767.
Impact Factor: 2.425
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* A low-cost open-architecture taste delivery system for gustatory fMRI and BCI experiments (473 views)
J Neurosci Methods (ISSN: 0165-0270, 1872-678xelectronic, 0165-0270linking), 2019 Jan 1; 311: 1-12.
Impact Factor: 2.668
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Sciacca MFM, Tempra C, Scollo F, Milardi D, La Rosa C
* Amyloid growth and membrane damage: Current themes and emerging perspectives from theory and experiments on Abeta and hIAPP (232 views) (PDF 107 views)
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Impact Factor: 4.647
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Granata D, Amato U, Alfano B
* MRI denoising by nonlocal means on multi-GPU (315 views)
J Real-Time Image Pr (ISSN: 1861-8200), 2016; N/D: 1-11.
Impact Factor: 2.01
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Vitiello G, Falanga A, Petruk AA, Merlino A, Fragneto G, Paduano L, Galdiero S, D'Errico G
* Fusion of raft-like lipid bilayers operated by a membranotropic domain of the HSV-type I glycoprotein gH occurs through a cholesterol-dependent mechanism (381 views)
Soft Matter (ISSN: 1744-683x), 2015; 11(15): 3003-3016.
Impact Factor: 3.798
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Marasco D, Messori L, Marzo T, Merlino A
* Oxaliplatin vs. cisplatin: Competition experiments on their binding to lysozyme (724 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9226linking), 2015; 44(22): 10392-10398.
Impact Factor: 4.177
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Tomasello MF, Sinopoli A, Attanasio F, Giuffrida ML, Campagna T, Milardi D, Pappalardo G
* Molecular and cytotoxic properties of hIAPP17-29 and rIAPP17-29 fragments: A comparative study with the respective full-length parent polypeptides (1043 views)
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Impact Factor: 3.447
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Galdiero S, Falanga A, Cantisani M, Vitiello M, Morelli G, Galdiero M
* Peptide-Lipid Interactions: Experiments and Applications (1012 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2013 Sep; 14(9): 18758-18789.
Impact Factor: 2.339
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Travaglia A, Satriano C, Giuffrida ML, La Mendola D, Rampazzo E, Prodi L, Rizzarelli E
* Electrostatically driven interaction of silica-supported lipid bilayer nanoplatforms and a nerve growth factor-mimicking peptide (338 views)
Soft Matter (ISSN: 1744-683x), 2013; 9(18): 4648-4654.
Impact Factor: 4.151
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Faiella M, Maglio O, Nastri F, Lombardi A, Lista L, Hagen WR, Pavone V
* De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein (474 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2012 Dec 7; 18(50): 15960-15971.
Impact Factor: 5.831
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Merlino A, Vitiello G, Grimaldi M, Sica F, Busi E, Basosi R, D’Ursi A, Fragneto G, Paduano L, D’Errico G
* Destabilization of Lipid Membranes by a Peptide Derived from Glycoprotein gp36 of Feline Immunodeficiency Virus: A Combined Molecular Dynamics/Experimental Study (470 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2012 Jan 12; 116(1): 401-412.
Impact Factor: 3.607
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D'Errico G, Ercole C, Lista M, Pizzo E, Falanga A, Galdiero S, Spadaccini R, Picone D
* Enforcing the positive charge of N-termini enhances membrane interaction and antitumor activity of bovine seminal ribonuclease (478 views)
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Impact Factor: 3.99
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Verardi R, Traaseth NJ, Shi L, Porcelli F, Monfregola L, De Luca S, Amodeo P, Veglia G, Scaloni A
* Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers (486 views)
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Impact Factor: 3.99
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BETOCCHI S, PACE L, VILLARI B, ALFANO B, CIARMIELLO A, SALVATORE M, CHIARIELLO M
* The T2K experiment (597 views)
Nucl Instrum Meth A (ISSN: 0168-9002), 2011; 659(1): 106-135.
Impact Factor: 1.207
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Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (494 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
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Improta R, Barone V, Lami A, Santoro F
* Quantum dynamics of the ultrafast ππ*/nπ* population transfer in uracil and 5-fluoro-uracil in water and acetonitrile (289 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2009 Oct 29; 113(43): 14491-14503.
Impact Factor: 3.471
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Grasso G, D'Agata R, Zanoli L, Spoto G
* Microfluidic networks for surface plasmon resonance imaging real-time kinetics experiments (271 views)
Microchemical Journal (ISSN: 0026-265x), 2009 Sep; 93(1): 82-86.
Impact Factor: 2.579
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Hilvo M, Baranauskiene L, Salzano AM, Scaloni A, Matulis D, Innocenti A, Scozzafava A, Monti SM, Di Fiore A, De Simone G, Lindfors M, Janis J, Valjakka J, Pastorekova S, Pastorek J, Kulomaa MS, Nordlund HR, Supuran CT, Parkkila S
* Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes (459 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 10; 283(41): 27799-27809.
Impact Factor: 5.52
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Sciacca MFM, Pappalardo M, Milardi D, Grasso DM, La Rosa C
* Calcium-Activated Membrane Interaction Of The Islet Amyloid Polypeptide: Implications In The Pathogenesis Of Type Ii Diabetes Mellitus (962 views)
Arch Biochem Biophys, 2008 Sep 15; 65(1-2): 291-298.
Impact Factor: 3.043
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Vaccaro M, Accardo A, D'Errico G, Schillen K, Radulescu A, Tesauro D, Morelli G, Paduano L
* Peptides and gd complexes containing colloidal assemblies as tumor-specific contrast agents in MRI: Physicochemical characterization (399 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2007 Sep; 93(5): 1736-1746.
Impact Factor: 4.627
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Pappalardo G, Milardi D, Magrì A, Attanasio F, Impellizzeri G, La Rosa C, Grasso D, Rizzarelli E
* Environmental factors differently affect human and rat IAPP: Conformational preferences and membrane interactions of IAPP17-29 peptide derivatives (592 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2007; 13(36): 10204-10215.
Impact Factor: 5.33
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Saporito A, Marasco D, Chambery A, Botti P, Monti SM, Pedone C, Ruvo M
* The chemical synthesis of the GstI protein by NCL on a X-Met site (642 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2006 Dec 5; 83(5): 508-518.
Impact Factor: 2.48
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Vacatello M, D'Auria G, Falcigno L, Dettin M, Gambaretto R, Di Bello C, Paolillo L
* Conformational Analysis Of Novel Heparin Binding Peptides (618 views)
Biomaterials (ISSN: 0142-9612, 1878-5905electronic, 0142-9612linking), 2005 Jun; 26(16): 3207-3214.
Impact Factor: 4.698
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De Luca S, Sanseverino M, Zocchi I, Pedone C, Morelli G, Ragone R
* Receptor fragment approach to the binding between CCK8 peptide and cholecystokinin receptors: A fluorescence study on type B receptor fragment CCKB-R (352-379) (359 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2005 Mar; 77(4): 205-211.
Impact Factor: 2.545
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Improta R, Antonello S, Formaggio F, Maran F, Rega N, Barone V
* Understanding Electron Transfer across Negatively-Charged Aib Oligopeptides (575 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2005 Jan 20; 109(2): 1023-1033.
Impact Factor: 4.033
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Bonomo RP, Cucinotta V, Giuffrida A, Impellizzeri G, Magrì A, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
* A re-investigation of copper coordination in the octa-repeats region of the prion protein (376 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2005 Jan 7; (1): 150-158.
Impact Factor: 3.003
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Calhoun JR, Nastri F, Maglio O, Pavone V, Lombardi A, Degrado WF
* Artificial diiron proteins: From structure to function (480 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2005; 80(2-3): 264-278.
Impact Factor: 2.545
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Berisio R, Granata V, Vitagliano L, Zagari A
* Imino acids and collagen triple helix stability: Characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats (437 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2004 Sep 22; 126(37): 11402-11403.
Impact Factor: 6.903
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De Capua A, Del Gatto A, Zaccaro L, Saviano G, Carlucci A, Livigni A, Gedressi C, Tancredi T, Pedone C, Saviano M
* A synthetic peptide reproducing the mitochondrial targeting motif of AKAP121: A conformational study (460 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 459-466.
Impact Factor: 2.863
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Improta R, Barone V
* Assesing the reliability of density functional methods in the conformational study of polypeptides: The treatment of intraresidue nonbonding interactions (405 views)
J Comput Chem (ISSN: 0192-8651, 1096-987xelectronic), 2004; 25(11): 1333-1341.
Impact Factor: 3.168
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Zarivach R, Bashan A, Berisio R, Harms J, Auerbach T, Schluenzen F, Bartels H, Baram D, Pyetan E, Sittner A, Amit M, Hansen HAS, Kessler M, Liebe C, Wolff A, Agmon I, Yonath A
* Functional aspects of ribosomal architecture: Symmetry, chirality and regulation (430 views)
J Phys Org Chem (ISSN: 0894-3230), 2004; 17(11): 901-912.
Impact Factor: 1.211
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Galdiero S, Vitiello M, D'Isanto M, Di Niola E, Peluso L, Raieta K, Pedone C, Galdiero M, Benedetti E
* Induction of signaling pathways by herpes simplex virus type 1 through glycoprotein H peptides (589 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 494-502.
Impact Factor: 2.863
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Mangiapia G, Accardo A, Celso FL, Tesauro D, Morelli G, Radulescu A, Paduano L
* Mixed micelles composed of peptides and gadolinium complexes as tumor-specific contrast agents in MRI: A sans study (587 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2004; 108(45): 17611-17617.
Impact Factor: 3.834
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Musumeci D, Roviello GN, Valente M, Sapio R, Pedone C, Bucci EM
* New synthesis of PNA-3′DNA linker monomers, useful building blocks to obtain PNA/DNA chimeras (429 views)
Biopolymers, 2004; 76(6): 535-542.
Impact Factor: 2.248
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Mansi R, Tesauro D, De Capua A, Fattorusso R, Carac C, Aloj L, Benedetti E, Morelli G
* Peptide-chelating agent conjugate for selective targeting of somatostatin receptor type 1: Synthesis and characterization (472 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 527-534.
Impact Factor: 2.863
View Export to BibTeX Export to EndNote
Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (544 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
View Export to BibTeX Export to EndNote
Bonomo RP, Bruno V, Conte E, De Guidi G, La Mendola D, Maccarrone G, Nicoletti F, Rizzarelli E, Sortino S, Vecchio G
* Potentiometric, spectroscopic and antioxidant activity studies of SOD mimics containing carnosine (385 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2003; (23): 4406-4415.
Impact Factor: 2.908
View Export to BibTeX Export to EndNote
Improta R, Mele F, Crescenzi O, Benzi C, Barone V
* Understanding the role of stereoelectronic effects in determining collagen stability. 2. A quantum mechanical/molecular mechanical study of (Proline-Proline-Glycine)n polypeptides (340 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2002 Jul 3; 124(26): 7857-7865.
Impact Factor: 6.201
View Export to BibTeX Export to EndNote
Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
* Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95 (384 views)
J Cryst Growth (ISSN: 0022-0248), 2001; 232(1-4): 481-488.
Impact Factor: 1.283
View Export to BibTeX Export to EndNote
Berisio R, Vitagliano L, Mazzarella L, Zagari A
Crystal Structure Of A Collagen-Like Polypeptide With Repeating Sequence Pro-Hyp-Gly At 1. 4 Ang Resolution: Implications For Collagen Hydration (436 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 8-13.
Impact Factor: 2.405
View Export to BibTeX Export to EndNote
D'Andrea LD, Mazzeo M, Isernia C, Rossi F, Saviano M, Gallo P, Paolillo L, Pedone C
Solution conformational preferences of a peptidic analogue of a natural macrolide (381 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(3): 349-361.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Zanotti G, Maione A, Rossi F, Saviano M, Pedone C, Tancredi T
BIOACTIVE PEPTIDES - CONFORMATIONAL STUDY OF A CYSTINYL CYCLOHEPTAPEPTIDE IN ITS FREE AND CALCIUM COMPLEXED FORMS (581 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1993 Jul; 33(7): 1083-1091.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Di Blasio B, Lombardi A, D'Auria G, Saviano M, Isernia C, Maglio O, Paolillo L, Pedone C, Pavone V
Beta-Alanine Containing Peptides: Gamma-Turns In Cyclotetrapeptides (560 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1993 Apr; 31(10): 621-631.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Pavone V, Lombardi A, D'Auria G, Saviano M, Nastri F, Paolillo L, Di Blasio B, Pedone C
β-Alanine containing peptides: A novel molecular tool for the design of γ-turns (813 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1992 Feb; 32(2): 173-184.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Tancredi T, Benedetti E, Grimaldi M, Pedone C, Rossi F, Saviano M, Temussi PA, Zanotti G
Ion binding of cyclolinopeptide A: An NMR and CD conformational study (633 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1991 May; 31(6): 761-767.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
44 Records (44 excluding Abstracts).
Total impact factor: 146.947 (146.947 excluding Abstracts).
Total 5 year impact factor: 164.9 (164.9 excluding Abstracts).
Total impact factor: 146.947 (146.947 excluding Abstracts).
Total 5 year impact factor: 164.9 (164.9 excluding Abstracts).
513 views. Last view on Sunday 19 March 2023, 7:08:40
ibb.cnr.it
