Structure and biological activity of a conformational constrained apolipoprotein A-I-derived helical peptide targeting the protein haptoglobin (401 views)
Rsc Adv (ISSN: 2046-2069), 2014; 4(93): 51353-51361.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.84, 5-year impact factor: 3.907
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84908242596&partnerID=40&md5=0f74360c110fa4dc4808b6ab9c6a814f
Keywords: Apolipoprotein A-I, Helical Peptide,
Affiliations:
*** IBB - CNR ***
Dipartimento di Biologia, Università di Napoli Federico II, Via Mezzocannone 8Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16Napoli, Italy
Istituto per Il Sistema Produzione Animale in Ambiente Mediterraneo, CNR, via ArgineNapoli, Italy
Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Università di Napoli, via Vivaldi 43Caserta, Italy
References:
Joy, T., Hegele, R.A., Is raising HDL a futile strategy for atheroprotection? (2008) Nat. Rev. Drug Discovery, 7, pp. 143-15
Linsel-Nitschke, P., Tall, A.R., HDL as a target in the treatment of atherosclerotic cardiovascular disease (2005) Nat. Rev. Drug Discovery, 4, pp. 193-205
Wang, M., Briggs, M.R., HDL: The metabolism, function, and therapeutic importance (2004) Chem. Rev., 104, pp. 119-137
Davidson, W.S., Thompson, T.B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem., 282, pp. 22249-22253
Thomas, M.J., Bhat, S., Sorci-Thomas, M.G., Three-dimensional models of HDL ApoA-I: Implications for its assembly and function (2008) J. Lipid Res., 49, pp. 1875-1883
Sevugan Chetty, P., Mayne, L., Kan, Z.Y., Lund-Katz, S., Englander, S.W., Phillips, M.C., Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry (2012) Proc. Natl. Acad. Sci. U. S. A., 109, pp. 11687-11692
Phillips, M.C., New insights into the determination of HDL structure by apolipoproteins (2013) J. Lipid Res., 54, pp. 2034-2048
Balestrieri, M., Cigliano, L., Simone, M.L., Dale, B., Abrescia, P., Haptoglobin inhibits lecithin-cholesterol acyltransferase in human ovarian follicular fluid (2001) Mol. Reprod. Dev., 59, pp. 186-191
Spagnuolo, M.S., Cigliano, L., D'Andrea, L.D., Pedone, C., Abrescia, P., Assignment of the binding site for haptoglobin on apolipoprotein A-I (2005) J. Biol. Chem., 280, pp. 1193-1198
Cigliano, L., Pugliese, C.R., Spagnuolo, M.S., Palumbo, R., Abrescia, P., Haptoglobin binds the antiatherogenic protein apolipoprotein E-impairment of apolipoprotein e stimulation of both lecithin-cholesterol acyltransferase activity and cholesterol uptake by hepatocytes (2009) FEBS J., 276, pp. 6158-6171
Bucci, M., Cigliano, L., Vellecco, V., D'Andrea, L.D., Ziaco, B., Rossi, A., Sautebin, L., Cirino, G., Apolipoprotein A-I (ApoA-I) mimetic peptide P2a by restoring cholesterol esterification unmasks ApoA-I anti-inflammatory endogenous activity in vivo (2012) J. Pharmacol. Exp. Ther., 340, pp. 716-722
Karle, I.L., Balaram, P., Structural characteristics of alpha-helical peptide molecules containing Aib residues (1990) Biochemistry, 29, pp. 6747-6756
Bashtovyy, D., Jones, M.K., Anantharamaiah, G.M., Segrest, J.P., Sequence conservation of apolipoprotein A-I affords novel insights into HDL structure-function (2011) J. Lipid Res., 52, pp. 435-450
Kaul, R., Balaram, P., Stereochemical control of peptide folding (1999) Bioorg. Med. Chem., 7, pp. 105-117
Tyndall, J.D., Nall, T., Fairlie, D.P., Proteases universally recognize beta strands in their active sites (2005) Chem. Rev., 105, pp. 973-999
Toniolo, C., Formaggio, F., Crisma, M., Bonora, G.M., Pegoraro, S., Polinelli, S., Boesten, W.H.J., Kamphuis, J., Synthesis, characterization and solution conformational analysis of Cα-methyl, Cα-benzylglycine[(αMe)Phe] model peptides (1991) Pept. Res., 5, pp. 56-61
Greenfield, N.J., Using circular dichroism spectra to estimate protein secondary structure (2007) Nat. Protoc., 1, pp. 2876-2890
Wuthrich, K., Protein structure determination in solution by nuclear magnetic resonance spectroscopy (1989) Science, 243, pp. 45-50
Wishart, D.S., Sykes, B.D., Richards, F.M., Relationship between nuclear magnetic resonance chemical shift and protein secondary structure (1991) J. Mol. Biol., 222, pp. 311-333
Herrmann, T., Guntert, P., Wuthrich, K., Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA (2002) J. Mol. Biol., 319, pp. 209-227
Mayer, M., Meyer, B., Group epitope mapping by saturation transfer difference NMR to identify the segments of a ligand, which is in direct contact with a protein receptor (2001) J. Am. Chem. Soc., 123, pp. 6108-6117
Meyer, B., Peters, T., NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors (2003) Angew. Chem., Int. Ed., 42, pp. 864-890
Clore, G.M., Gronenborn, A.M., Theory of the time dependent transferred nuclear Overhauser effect: Application to the structural analysis of ligand-protein complexes in solution (1983) J. Magn. Reson., 53, pp. 423-442
Kumar, A., Wagner, G., Ernst, R.R., Wutrich, K., Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: Implications for the studies of protein conformation (1981) J. Am. Chem. Soc., 103, pp. 3654-3658
Langlois, M.R., Delanghe, J.R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem., 42, pp. 1589-1600
Anthis, N.J., Clore, G.M., Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm (2013) Protein Sci., 22, pp. 851-858
Goddard, T.D., Kneller, D.G., SPARKY 3, , University of California, San Francisco
Masse, J.E., Keller, R., AutoLink: Automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic (2005) J. Magn. Reson., 174, pp. 133-151
Koradi, R., Billeter, M., Wuthrich, K., MOLMOL: A program for the display and analysis of macromolecular structures (1996) J. Mol. Graphics, 14, pp. 29-32
Guex, N., Peitsch, M.C., SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling (1997) Electrophoresis, 18, pp. 2714-2723
Scott, W.R.P., Huenenberger, P.H., Tironi, I.G., Mark, A.E., Billeter, S.R., Fennen, J., Torda, A.E., Van Gunsteren, W.F., The GROMOS biomolecular simulation program package (1999) J. Phys. Chem. A, 103, pp. 3596-3607
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Cigliano, L., Spagnuolo, M.S., Abrescia, P., Quantitative variations of the isoforms in haptoglobin 1-2 and 2-2 individual phenotypes (2003) Arch. Biochem. Biophys., 416, pp. 227-237
Porta, A., Cassano, E., Balestrieri, M., Bianco, M., Picone, R., De Stefano, C., Abrescia, P., Haptoglobin transport into human ovarian follicles and its binding to apolipoprotein A-1 (1999) Zygote, 7, pp. 67-77
Chen, C.H., Albers, J.J., Characterization of proteoliposomes containing apoprotein A-I: A new substrate for the measurement of lecithin-cholesterol acyltransferase activity (1982) J. Lipid Res., 23, pp. 680-691
Davidson, W. S., Thompson, T. B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem., 282, pp. 22249-22253
Thomas, M. J., Bhat, S., Sorci-Thomas, M. G., Three-dimensional models of HDL ApoA-I: Implications for its assembly and function (2008) J. Lipid Res., 49, pp. 1875-1883
Phillips, M. C., New insights into the determination of HDL structure by apolipoproteins (2013) J. Lipid Res., 54, pp. 2034-2048
Spagnuolo, M. S., Cigliano, L., D'Andrea, L. D., Pedone, C., Abrescia, P., Assignment of the binding site for haptoglobin on apolipoprotein A-I (2005) J. Biol. Chem., 280, pp. 1193-1198
Karle, I. L., Balaram, P., Structural characteristics of alpha-helical peptide molecules containing Aib residues (1990) Biochemistry, 29, pp. 6747-6756
Tyndall, J. D., Nall, T., Fairlie, D. P., Proteases universally recognize beta strands in their active sites (2005) Chem. Rev., 105, pp. 973-999
Greenfield, N. J., Using circular dichroism spectra to estimate protein secondary structure (2007) Nat. Protoc., 1, pp. 2876-2890
Wishart, D. S., Sykes, B. D., Richards, F. M., Relationship between nuclear magnetic resonance chemical shift and protein secondary structure (1991) J. Mol. Biol., 222, pp. 311-333
Clore, G. M., Gronenborn, A. M., Theory of the time dependent transferred nuclear Overhauser effect: Application to the structural analysis of ligand-protein complexes in solution (1983) J. Magn. Reson., 53, pp. 423-442
Langlois, M. R., Delanghe, J. R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem., 42, pp. 1589-1600
Anthis, N. J., Clore, G. M., Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm (2013) Protein Sci., 22, pp. 851-858
Goddard, T. D., Kneller, D. G., SPARKY 3, , University of California, San Francisco
Masse, J. E., Keller, R., AutoLink: Automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic (2005) J. Magn. Reson., 174, pp. 133-151
Scott, W. R. P., Huenenberger, P. H., Tironi, I. G., Mark, A. E., Billeter, S. R., Fennen, J., Torda, A. E., Van Gunsteren, W. F., The GROMOS biomolecular simulation program package (1999) J. Phys. Chem. A, 103, pp. 3596-3607
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Chen, C. H., Albers, J. J., Characterization of proteoliposomes containing apoprotein A-I: A new substrate for the measurement of lecithin-cholesterol acyltransferase activity (1982) J. Lipid Res., 23, pp. 680-691
Rsc Adv (ISSN: 2046-2069), 2014; 4(93): 51353-51361.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.84, 5-year impact factor: 3.907
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84908242596&partnerID=40&md5=0f74360c110fa4dc4808b6ab9c6a814f
Keywords: Apolipoprotein A-I, Helical Peptide,
Affiliations:
*** IBB - CNR ***
Dipartimento di Biologia, Università di Napoli Federico II, Via Mezzocannone 8Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16Napoli, Italy
Istituto per Il Sistema Produzione Animale in Ambiente Mediterraneo, CNR, via ArgineNapoli, Italy
Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Università di Napoli, via Vivaldi 43Caserta, Italy
References:
Joy, T., Hegele, R.A., Is raising HDL a futile strategy for atheroprotection? (2008) Nat. Rev. Drug Discovery, 7, pp. 143-15
Linsel-Nitschke, P., Tall, A.R., HDL as a target in the treatment of atherosclerotic cardiovascular disease (2005) Nat. Rev. Drug Discovery, 4, pp. 193-205
Wang, M., Briggs, M.R., HDL: The metabolism, function, and therapeutic importance (2004) Chem. Rev., 104, pp. 119-137
Davidson, W.S., Thompson, T.B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem., 282, pp. 22249-22253
Thomas, M.J., Bhat, S., Sorci-Thomas, M.G., Three-dimensional models of HDL ApoA-I: Implications for its assembly and function (2008) J. Lipid Res., 49, pp. 1875-1883
Sevugan Chetty, P., Mayne, L., Kan, Z.Y., Lund-Katz, S., Englander, S.W., Phillips, M.C., Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry (2012) Proc. Natl. Acad. Sci. U. S. A., 109, pp. 11687-11692
Phillips, M.C., New insights into the determination of HDL structure by apolipoproteins (2013) J. Lipid Res., 54, pp. 2034-2048
Balestrieri, M., Cigliano, L., Simone, M.L., Dale, B., Abrescia, P., Haptoglobin inhibits lecithin-cholesterol acyltransferase in human ovarian follicular fluid (2001) Mol. Reprod. Dev., 59, pp. 186-191
Spagnuolo, M.S., Cigliano, L., D'Andrea, L.D., Pedone, C., Abrescia, P., Assignment of the binding site for haptoglobin on apolipoprotein A-I (2005) J. Biol. Chem., 280, pp. 1193-1198
Cigliano, L., Pugliese, C.R., Spagnuolo, M.S., Palumbo, R., Abrescia, P., Haptoglobin binds the antiatherogenic protein apolipoprotein E-impairment of apolipoprotein e stimulation of both lecithin-cholesterol acyltransferase activity and cholesterol uptake by hepatocytes (2009) FEBS J., 276, pp. 6158-6171
Bucci, M., Cigliano, L., Vellecco, V., D'Andrea, L.D., Ziaco, B., Rossi, A., Sautebin, L., Cirino, G., Apolipoprotein A-I (ApoA-I) mimetic peptide P2a by restoring cholesterol esterification unmasks ApoA-I anti-inflammatory endogenous activity in vivo (2012) J. Pharmacol. Exp. Ther., 340, pp. 716-722
Karle, I.L., Balaram, P., Structural characteristics of alpha-helical peptide molecules containing Aib residues (1990) Biochemistry, 29, pp. 6747-6756
Bashtovyy, D., Jones, M.K., Anantharamaiah, G.M., Segrest, J.P., Sequence conservation of apolipoprotein A-I affords novel insights into HDL structure-function (2011) J. Lipid Res., 52, pp. 435-450
Kaul, R., Balaram, P., Stereochemical control of peptide folding (1999) Bioorg. Med. Chem., 7, pp. 105-117
Tyndall, J.D., Nall, T., Fairlie, D.P., Proteases universally recognize beta strands in their active sites (2005) Chem. Rev., 105, pp. 973-999
Toniolo, C., Formaggio, F., Crisma, M., Bonora, G.M., Pegoraro, S., Polinelli, S., Boesten, W.H.J., Kamphuis, J., Synthesis, characterization and solution conformational analysis of Cα-methyl, Cα-benzylglycine[(αMe)Phe] model peptides (1991) Pept. Res., 5, pp. 56-61
Greenfield, N.J., Using circular dichroism spectra to estimate protein secondary structure (2007) Nat. Protoc., 1, pp. 2876-2890
Wuthrich, K., Protein structure determination in solution by nuclear magnetic resonance spectroscopy (1989) Science, 243, pp. 45-50
Wishart, D.S., Sykes, B.D., Richards, F.M., Relationship between nuclear magnetic resonance chemical shift and protein secondary structure (1991) J. Mol. Biol., 222, pp. 311-333
Herrmann, T., Guntert, P., Wuthrich, K., Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA (2002) J. Mol. Biol., 319, pp. 209-227
Mayer, M., Meyer, B., Group epitope mapping by saturation transfer difference NMR to identify the segments of a ligand, which is in direct contact with a protein receptor (2001) J. Am. Chem. Soc., 123, pp. 6108-6117
Meyer, B., Peters, T., NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors (2003) Angew. Chem., Int. Ed., 42, pp. 864-890
Clore, G.M., Gronenborn, A.M., Theory of the time dependent transferred nuclear Overhauser effect: Application to the structural analysis of ligand-protein complexes in solution (1983) J. Magn. Reson., 53, pp. 423-442
Kumar, A., Wagner, G., Ernst, R.R., Wutrich, K., Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: Implications for the studies of protein conformation (1981) J. Am. Chem. Soc., 103, pp. 3654-3658
Langlois, M.R., Delanghe, J.R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem., 42, pp. 1589-1600
Anthis, N.J., Clore, G.M., Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm (2013) Protein Sci., 22, pp. 851-858
Goddard, T.D., Kneller, D.G., SPARKY 3, , University of California, San Francisco
Masse, J.E., Keller, R., AutoLink: Automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic (2005) J. Magn. Reson., 174, pp. 133-151
Koradi, R., Billeter, M., Wuthrich, K., MOLMOL: A program for the display and analysis of macromolecular structures (1996) J. Mol. Graphics, 14, pp. 29-32
Guex, N., Peitsch, M.C., SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling (1997) Electrophoresis, 18, pp. 2714-2723
Scott, W.R.P., Huenenberger, P.H., Tironi, I.G., Mark, A.E., Billeter, S.R., Fennen, J., Torda, A.E., Van Gunsteren, W.F., The GROMOS biomolecular simulation program package (1999) J. Phys. Chem. A, 103, pp. 3596-3607
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Cigliano, L., Spagnuolo, M.S., Abrescia, P., Quantitative variations of the isoforms in haptoglobin 1-2 and 2-2 individual phenotypes (2003) Arch. Biochem. Biophys., 416, pp. 227-237
Porta, A., Cassano, E., Balestrieri, M., Bianco, M., Picone, R., De Stefano, C., Abrescia, P., Haptoglobin transport into human ovarian follicles and its binding to apolipoprotein A-1 (1999) Zygote, 7, pp. 67-77
Chen, C.H., Albers, J.J., Characterization of proteoliposomes containing apoprotein A-I: A new substrate for the measurement of lecithin-cholesterol acyltransferase activity (1982) J. Lipid Res., 23, pp. 680-691
Davidson, W. S., Thompson, T. B., The structure of apolipoprotein A-I in high density lipoproteins (2007) J. Biol. Chem., 282, pp. 22249-22253
Thomas, M. J., Bhat, S., Sorci-Thomas, M. G., Three-dimensional models of HDL ApoA-I: Implications for its assembly and function (2008) J. Lipid Res., 49, pp. 1875-1883
Phillips, M. C., New insights into the determination of HDL structure by apolipoproteins (2013) J. Lipid Res., 54, pp. 2034-2048
Spagnuolo, M. S., Cigliano, L., D'Andrea, L. D., Pedone, C., Abrescia, P., Assignment of the binding site for haptoglobin on apolipoprotein A-I (2005) J. Biol. Chem., 280, pp. 1193-1198
Karle, I. L., Balaram, P., Structural characteristics of alpha-helical peptide molecules containing Aib residues (1990) Biochemistry, 29, pp. 6747-6756
Tyndall, J. D., Nall, T., Fairlie, D. P., Proteases universally recognize beta strands in their active sites (2005) Chem. Rev., 105, pp. 973-999
Greenfield, N. J., Using circular dichroism spectra to estimate protein secondary structure (2007) Nat. Protoc., 1, pp. 2876-2890
Wishart, D. S., Sykes, B. D., Richards, F. M., Relationship between nuclear magnetic resonance chemical shift and protein secondary structure (1991) J. Mol. Biol., 222, pp. 311-333
Clore, G. M., Gronenborn, A. M., Theory of the time dependent transferred nuclear Overhauser effect: Application to the structural analysis of ligand-protein complexes in solution (1983) J. Magn. Reson., 53, pp. 423-442
Langlois, M. R., Delanghe, J. R., Biological and clinical significance of haptoglobin polymorphism in humans (1996) Clin. Chem., 42, pp. 1589-1600
Anthis, N. J., Clore, G. M., Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm (2013) Protein Sci., 22, pp. 851-858
Goddard, T. D., Kneller, D. G., SPARKY 3, , University of California, San Francisco
Masse, J. E., Keller, R., AutoLink: Automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic (2005) J. Magn. Reson., 174, pp. 133-151
Scott, W. R. P., Huenenberger, P. H., Tironi, I. G., Mark, A. E., Billeter, S. R., Fennen, J., Torda, A. E., Van Gunsteren, W. F., The GROMOS biomolecular simulation program package (1999) J. Phys. Chem. A, 103, pp. 3596-3607
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Chen, C. H., Albers, J. J., Characterization of proteoliposomes containing apoprotein A-I: A new substrate for the measurement of lecithin-cholesterol acyltransferase activity (1982) J. Lipid Res., 23, pp. 680-691
Structure and biological activity of a conformational constrained apolipoprotein A-I-derived helical peptide targeting the protein haptoglobin
The development of novel pharmacological treatments for atherosclerosis is an active research field in medicinal chemistry. It has been shown that the acute phase protein haptoglobin (Hpt) plays a role in modulating the reverse cholesterol transport binding to the HDL-major protein Apolipoprotein A-I, and it also plays a role in impairing the activity of the lecithin-cholesterol acyltransferase (LCAT). We reported that the peptide P2a in vitro and in vivo restores the LCAT activity in the presence of Hpt. Now, we have designed and characterized a conformational constrained P2a analogue, ApoAib, with the intention of improving Hpt binding and metabolic stability. Using non-proteogenic aminoisobutyric acid residues, we have obtained a well folded α-helical peptide with high proteolytic stability in serum. It binds to Hpt, impairs haptoglobin binding to HDL, and restores LCAT activity in the presence of haptoglobin. Furthermore, an interaction analysis using NMR revealed the peptide binding site involved in haptoglobin molecular recognition. In conclusion, ApoAib represents a promising candidate to improve reverse cholesterol transport for application in cardiovascular diseases. This journal is © the Partner Organisations 2014.
The development of novel pharmacological treatments for atherosclerosis is an active research field in medicinal chemistry. It has been shown that the acute phase protein haptoglobin (Hpt) plays a role in modulating the reverse cholesterol transport binding to the HDL-major protein Apolipoprotein A-I, and it also plays a role in impairing the activity of the lecithin-cholesterol acyltransferase (LCAT). We reported that the peptide P2a in vitro and in vivo restores the LCAT activity in the presence of Hpt. Now, we have designed and characterized a conformational constrained P2a analogue, ApoAib, with the intention of improving Hpt binding and metabolic stability. Using non-proteogenic aminoisobutyric acid residues, we have obtained a well folded α-helical peptide with high proteolytic stability in serum. It binds to Hpt, impairs haptoglobin binding to HDL, and restores LCAT activity in the presence of haptoglobin. Furthermore, an interaction analysis using NMR revealed the peptide binding site involved in haptoglobin molecular recognition. In conclusion, ApoAib represents a promising candidate to improve reverse cholesterol transport for application in cardiovascular diseases. This journal is © the Partner Organisations 2014.
Structure and biological activity of a conformational constrained apolipoprotein A-I-derived helical peptide targeting the protein haptoglobin
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Structure and biological activity of a conformational constrained apolipoprotein A-I-derived helical peptide targeting the protein haptoglobin
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Impact Factor: 4.001
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Basile A, Del Gatto A, Diana D, Di Stasi R, Falco A, Festa M, Rosati A, Barbieri A, Franco R, Arra C, Pedone C, Fattorusso R, Turco MC, D'Andrea LD
* Characterization of a designed vascular endothelial growth factor receptor antagonist helical peptide with antiangiogenic activity in vivo (559 views)
J Med Chem (ISSN: 1520-4804, 0022-2623, 0022-2623print), 2011 Mar 10; 54(5): 1391-1400.
Impact Factor: 5.248
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Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
* Structural analysis of a helical peptide unfolding pathway (507 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2010 May 10; 16(18): 5400-5407.
Impact Factor: 5.476
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Cigliano L, Pugliese CR, Spagnuolo MS, Palumbo R, Abrescia P
* Haptoglobin binds the antiatherogenic protein apolipoprotein e - Impairment of apolipoprotein e stimulation of both lecithin: Cholesterol acyltransferase activity and cholesterol uptake by hepatocytes (398 views)
Febs J (ISSN: 1742-464x), 2009 Nov; 276(21): 6158-6171.
Impact Factor: 3.042
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Cigliano L, D'Andrea LD, Maresca B, Serino M, Carlucci A, Salvatore A, Spagnuolo MS, Scigliuolo G, Pedone C, Abrescia P
* Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin (393 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1437-4315), 2008 Nov; 389(11): 1421-1426.
Impact Factor: 3.035
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Cigliano L, Maresca B, Salvatore A, Nino M, Monfrecola G, Ayala F, Carlucci A, Pugliese RC, Pedone C, Abrescia P
* Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity (418 views)
Journal Of The European Academy Of Dermatology And Venereology (ISSN: 1468-3083, 0926-9959), 2008 Apr; 22(4): 417-425.
Impact Factor: 2.276
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Salvatore A, Cigliano L, Bucci EM, Corpillo D, Velasco S, Carlucci A, Pedone C, Abrescia P
* Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase (495 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2007 Oct 2; 46(39): 11158-11168.
Impact Factor: 3.368
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D'Andrea LD, Iaccarino G, Fattorusso R, Sorriento D, Carannante C, Capasso D, Trimarco B, Pedone C
* Targeting angiogenesis: Structural characterization and biological properties of a de novo engineered VEGF mimicking peptide (657 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2005 Oct 4; 102(40): 14215-14220.
Impact Factor: 10.231
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Spagnuolo MS, Cigliano L, D'Andrea LD, Pedone C, Abrescia P
* Assignment of the binding site for haptoglobin on apolipoprotein A-I (503 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Jan 14; 280(2): 1193-1198.
Impact Factor: 5.854
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Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E, Santoro AM
Synthesis, spectroscopic characterisation, and metal ion interaction of a new α-helical peptide (491 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1998; 4(9): 1791-1798.
Impact Factor: 5.153
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* Cell milieu significantly affects the fate of AApoAI amyloidogenic variants: predestination or serendipity? (522 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2017 Nov 23; 1862(3): 377-384.
Impact Factor: 4.28
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Mercurio FA, Marasco D, Di Natale C, Pirone L, Costantini S, Pedone EM, Leone M
* Targeting EphA2-Sam and Its Interactome: Design and Evaluation of Helical Peptides Enriched in Charged Residues (416 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-4227linking), 2016 Nov 17; 17(22): 2179-2188.
Impact Factor: 2.847
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Scognamiglio PL, Di Natale C, Leone M, Cascella R, Cecchi C, Lirussi L, Antoniali G, Riccardi D, Morelli G, Tell G, Chiti F, Marasco D
* Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia (396 views)
Oncotarget (ISSN: 1949-2553, 1949-2553electronic, 1949-2553linking), 2016 Sep 13; 7(37): 59129-59143.
Impact Factor: 5.168
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Galdiero S, Falanga A, Berisio R, Grieco P, Morelli G, Galdiero M
* Antimicrobial peptides as an opportunity against bacterial diseases (762 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015 Mar 11; 22(14): 1665-1677.
Impact Factor: 3.455
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Spagnuolo MS, Di Stasi R, De Rosa L, Maresca B, Cigliano L, D'Andrea LD
* Analysis of the haptoglobin binding region on the apolipoprotein A-I-derived P2a peptide (376 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Apr; 19(4): 220-226.
Impact Factor: 1.862
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Ziaco B, Diana D, Capasso D, Palumbo R, Celentano V, Di Stasi R, Fattorusso R, D'Andrea LD
* C-terminal truncation of Vascular Endothelial Growth Factor mimetic helical peptide preserves structural and receptor binding properties (370 views)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2012 Jul 27; 424(2): 290-294.
Impact Factor: 2.406
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Bucci M, Cigliano L, Vellecco V, D'Andrea LD, Ziaco B, Rossi A, Sautebin L, Carlucci A, Abrescia P, Pedone C, Ianaro A, Cirino G
* Apolipoprotein A-I (ApoA-I) mimetic peptide P2a by restoring cholesterol esterification unmasks ApoA-I anti-inflammatory endogenous activity in vivo (476 views)
J Pharmacol Exp Ther (ISSN: 1521-0103, 0022-3565), 2012 Mar; 340(3): 716-722.
Impact Factor: 3.891
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Monti DM(1), Di Gaetano S, Del Giudice R, Giangrande C, Amoresano A, Monti M, Arciello A, Piccoli R
* Apolipoprotein A-I amyloidogenic variant L174S, expressed and isolated from stably transfected mammalian cells, is associated with fatty acids (325 views)
Amyloid (ISSN: 1350-6129), 2012 Mar; 19(1): 21-27.
Impact Factor: 4.436
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Raimondi S, Guglielmi F, Giorgetti S, Di Gaetano S, Arciello A, Monti DM, Relini A, Nichino D, Doglia SM, Natalello A, Pucci P, Mangione P, Obici L, Merlini G, Stoppini M, Robustelli P, Tartaglia GG, Vendruscolo M, Dobson CM, Piccoli R, Bellotti V
* Effects of the Known Pathogenic Mutations on the Aggregation Pathway of the Amyloidogenic Peptide of Apolipoprotein A-I (459 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2011 Apr 1; 407(3): 465-476.
Impact Factor: 4.001
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Basile A, Del Gatto A, Diana D, Di Stasi R, Falco A, Festa M, Rosati A, Barbieri A, Franco R, Arra C, Pedone C, Fattorusso R, Turco MC, D'Andrea LD
* Characterization of a designed vascular endothelial growth factor receptor antagonist helical peptide with antiangiogenic activity in vivo (559 views)
J Med Chem (ISSN: 1520-4804, 0022-2623, 0022-2623print), 2011 Mar 10; 54(5): 1391-1400.
Impact Factor: 5.248
View Export to BibTeX Export to EndNote
Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
* Structural analysis of a helical peptide unfolding pathway (507 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2010 May 10; 16(18): 5400-5407.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Cigliano L, Pugliese CR, Spagnuolo MS, Palumbo R, Abrescia P
* Haptoglobin binds the antiatherogenic protein apolipoprotein e - Impairment of apolipoprotein e stimulation of both lecithin: Cholesterol acyltransferase activity and cholesterol uptake by hepatocytes (398 views)
Febs J (ISSN: 1742-464x), 2009 Nov; 276(21): 6158-6171.
Impact Factor: 3.042
View Export to BibTeX Export to EndNote
Cigliano L, D'Andrea LD, Maresca B, Serino M, Carlucci A, Salvatore A, Spagnuolo MS, Scigliuolo G, Pedone C, Abrescia P
* Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin (393 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1437-4315), 2008 Nov; 389(11): 1421-1426.
Impact Factor: 3.035
View Export to BibTeX Export to EndNote
Cigliano L, Maresca B, Salvatore A, Nino M, Monfrecola G, Ayala F, Carlucci A, Pugliese RC, Pedone C, Abrescia P
* Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity (418 views)
Journal Of The European Academy Of Dermatology And Venereology (ISSN: 1468-3083, 0926-9959), 2008 Apr; 22(4): 417-425.
Impact Factor: 2.276
View Export to BibTeX Export to EndNote
Salvatore A, Cigliano L, Bucci EM, Corpillo D, Velasco S, Carlucci A, Pedone C, Abrescia P
* Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase (495 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2007 Oct 2; 46(39): 11158-11168.
Impact Factor: 3.368
View Export to BibTeX Export to EndNote
D'Andrea LD, Iaccarino G, Fattorusso R, Sorriento D, Carannante C, Capasso D, Trimarco B, Pedone C
* Targeting angiogenesis: Structural characterization and biological properties of a de novo engineered VEGF mimicking peptide (657 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2005 Oct 4; 102(40): 14215-14220.
Impact Factor: 10.231
View Export to BibTeX Export to EndNote
Spagnuolo MS, Cigliano L, D'Andrea LD, Pedone C, Abrescia P
* Assignment of the binding site for haptoglobin on apolipoprotein A-I (503 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Jan 14; 280(2): 1193-1198.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E, Santoro AM
Synthesis, spectroscopic characterisation, and metal ion interaction of a new α-helical peptide (491 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1998; 4(9): 1791-1798.
Impact Factor: 5.153
View Export to BibTeX Export to EndNote
18 Records (18 excluding Abstracts).
Total impact factor: 76.029 (76.029 excluding Abstracts).
Total 5 year impact factor: 74.925 (74.925 excluding Abstracts).
Total impact factor: 76.029 (76.029 excluding Abstracts).
Total 5 year impact factor: 74.925 (74.925 excluding Abstracts).
401 views. Last view on Monday 13 March 2023, 18:34:44
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