Molecular engineering of RANTES peptide mimetics with potent anti-HIV-1 activity (568 views)
Faseb J (ISSN: 0892-6638, 0892-6638linking), 2011 Apr; 25(4): 1230-1243.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.712, 5-year impact factor: 6.34
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79954597305&partnerID=40&md5=b2901bd84e7c3fc1a2ff38f2486ce3d5
Keywords: Aids, Antivirals, Ccr5, Chemokines, Rational Design, Viral Receptors, Chemokine Receptor Ccr5, Chemokine Receptor Cxcr4, Guanine Nucleotide Binding Protein, Rantes, Algorithm, Alpha Helix, Antiviral Activity, Article, Beta 1 Protein Strand, Carboxy Terminal Sequence, Computer Model, Human Immunodeficiency Virus 1, Hydrophobicity, N Loop, Nuclear Magnetic Resonance, Priority Journal, Protein Structure, Amino Acid Sequence, Anti-Hiv Agents, Biomimetic Materials, Chemokine Ccl5, Chemotaxis, Hydrophobic And Hydrophilic Interactions, Biomolecular, P38 Mitogen-Activated Protein Kinases, Peptides, Protein Conformation, Protein Engineering, Signal Transduction, Structure-Activity Relationship,
Affiliations:
*** IBB - CNR ***
Unit of Human Virology, Department of Biological and Technological Research (DIBIT), San Raffaele Scientific Institute, Milan, Italy
Department of Biomedical Sciences, University of Cagliari, Cagliari, Italy
National Research Council (CNR), Istituto di Chimica del Riconoscimento Molecolare (ICRM), Milan, Italy
Department of Chemistry, University of Naples Federico II, Naples, Italy
Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 10 Center Dr., Bethesda, MD 20892, United States
Istituto di Biostrutture e Bioimmagini (IBB), National Research Council (CNR), 80134 Napoli, Italy
References:
Berger, E.A., Murphy, P.M., Farber, J.M., Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease (1999) Annual Review of Immunology, 17, pp. 657-700. , DOI 10.1146/annurev.immunol.17.1.65
Lusso, P., HIV and the chemokine system: 10 years later (2006) EMBO J., 25, pp. 447-456
Lederman, M.M., Penn-Nicholson, A., Cho, M., Mosier, D., Biology of CCR5 and its role in HIV infection and treatment (2006) Journal of the American Medical Association, 296 (7), pp. 815-826. , http://jama.ama-assn.org/cgi/reprint/296/7/815, DOI 10.1001/jama.296.7.815
Strizki, J.M., Xu, S., Wagner, N.E., Wojcik, L., Liu, J., Hou, Y., Endres, M., Baroudy, B.M., SCH-C (SCH 351125), an orally bioavailable, small molecule antagonist of the chemokine receptor CCR5, is a potent inhibitor of HIV-1 infection in vitro and in vivo (2001) Proceedings of the National Academy of Sciences of the United States of America, 98 (22), pp. 12718-12723. , DOI 10.1073/pnas.221375398
Strizki, J.M., Tremblay, C., Xu, S., Wojcik, L., Wagner, N., Gonsiorek, W., Hipkin, R.W., Baroudy, B.M., Discovery and characterization of vicriviroc (SCH 417690), a CCR5 antagonist with potent activity against human immunodeficiency virus type 1 (2005) Antimicrobial Agents and Chemotherapy, 49 (12), pp. 4911-4919. , DOI 10.1128/AAC.49.12.4911-4919.2005
Watson, C., Jenkinson, S., Kazmierski, W., Kenakin, T., The CCR5 receptor-based mechanism of action of 873140, a potent allosteric noncompetitive HIV entry inhibitor (2005) Molecular Pharmacology, 67 (4), pp. 1268-1282. , DOI 10.1124/mol.104.008565
Meanwell, N.A., Kadow, J.F., Maraviroc, a chemokine CCR5 receptor antagonist for the treatment of HIV infection and AIDS (2007) Current Opinion in Investigational Drugs, 8 (8), pp. 669-681
Gulick, R.M., Lalezari, J., Goodrich, J., Clumeck, N., DeJesus, E., Horban, A., Nadler, J., Mayer, H., Maraviroc for previously treated patients with R5 HIV-1 infection (2008) N. Engl. J. Med., 359, pp. 1429-1441. , MOTIVATE Study Teams
Nardese, V., Longhi, R., Polo, S., Sironi, F., Arcelloni, C., Paroni, R., Desantis, C., Lusso, P., Structural determinants of CCR5 recognition and HIV-1 blockade in RANTES (2001) Nature Structural Biology, 8 (7), pp. 611-615. , DOI 10.1038/89653
Vangelista, L., Longhi, R., Sironi, F., Pavone, V., Lusso, P., Critical role of the N-loop and β1-strand hydrophobic clusters of RANTES-derived peptides in anti-HIV activity (2006) Biochemical and Biophysical Research Communications, 351 (3), pp. 664-668. , DOI 10.1016/j.bbrc.2006.10.090, PII S0006291X06023321
Skelton, N.J., Aspiras, F., Ogez, J., Schall, T.J., Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type (1995) Biochemistry, 34, pp. 5329-5342
Chung, C., Cooke, R.M., Proudfoot, A.E., Wells, T.N.C., The three-dimensional solution structure of RANTES (1995) Biochemistry, 34, pp. 9307-9314
Wilken, J., Hoover, D., Thompson, D.A., Barlow, P.N., McSparron, H., Picard, L., Wlodawer, A., Kent, S.B.H., Total chemical synthesis and high-resolution crystal structure of the potent anti-HIV protein AOP-RANTES (1999) Chemistry and Biology, 6 (1), pp. 43-51. , DOI 10.1016/S1074-5521(99)80019-2
Shaw, J.P., Johnson, Z., Borlat, F., Zwahlen, C., Kungl, A., Roulin, K., Harrenga, A., Proudfoot, A.E.I., The X-ray structure of RANTES: Heparin-derived disaccharides allows the rational design of chemokine inhibitors (2004) Structure, 12 (11), pp. 2081-2093. , DOI 10.1016/j.str.2004.08.014, PII S0969212604003430
Nussbaum, O., Broder, C.C., Berger, E.A., Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation (1994) Journal of Virology, 68 (9), pp. 5411-5422
Lusso, P., Cocchi, F., Balotta, C., Markham, P.D., Louie, A., Farci, P., Pal, R., Reitz Jr., M.S., Growth of macrophage-tropic and primary human immunodeficiency virus type 1 (HIV-1) isolates in a unique CD4 + T-cell clone (PM1): Failure to downregulate CD4 and to interfere with cell-line-tropic HIV-1 (1995) J. Virol., 69, pp. 3712-3720
Bax, A.D., Davis, D.G., MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy (1985) J. Magn. Res., 65, pp. 355-360
Jeener, J., Meier, B.H., Bachmann, P., Ernst, R.R., Investigation of exchange processes by two-dimensional NMR spectroscopy (1979) J. Chem. Phys., 71, pp. 4546-4553
Kumar, A., Wagner, G., Ernst, R.R., Wuthrich, K., Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy implications for studies of protein conformation (1981) J. Am. Chem. Soc., 103, pp. 3654-3658
Griesinger, C., Ernst, R.R., Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy (1978) Ø Magn. Res., 75, pp. 261-271
Piantini, U., Srensen, O.W., Ernst, R.R., Multiple quantum filters for elucidating NMR coupling networks (1982) J. Am. Chem. Soc., 104, pp. 6800-6801
Wuthrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley, New York
Marion, D., Wuthrich, K., Application of phase sensitive correlated spectroscopy (COSY) for measurements of proton-proton spin-spin coupling constants in proteins (1983) Biochem. Biophys. Res. Commun., 113, pp. 967-974
Hwang, T.L., Shaka, A.J., Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients (1995) J. Magn. Reson. Ser. A, 112, pp. 275-279
Keller, R., (2004) The Computer Aided Resonance Assignment Tutorial, , www.nmr.ch, ISBN 3-85600-112-3, CANTINA Verlag available from
Guntert, P., Braun, W., Wuthrich, K., Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA (1991) Journal of Molecular Biology, 217 (3), pp. 517-530
Guntert, P., Mumenthaler, C., Wuthrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) Journal of Molecular Biology, 273 (1), pp. 283-298. , DOI 10.1006/jmbi.1997.1284
Weiner Scott, J., Kollman Peter, A., Case David, A., Singh U.Chandra, Alagona Giuliano, Profeta Jr. Salvatore, Weiner Paul, Ghio Caterina, NEW FORCE FIELD FOR MOLECULAR MECHANICAL SIMULATION OF NUCLEIC ACIDS AND PROTEINS. (1984) Journal of the American Chemical Society, 106 (3), pp. 765-784
Weiner, S.J., Kollman, P.A., Nguyen, D.T., Case, D.A., An all atom force field for simulations of proteins and nucleic acids (1986) J. Comput. Chem., 7, pp. 230-252
Simons, K.T., Bonneau, R., Ruczinski, I., Baker, D., Ab initio protein structure prediction of CASP III targets using ROSETTA (1999) Proteins: Structure, Function and Genetics, 37 (SUPPL. 3), pp. 171-176. , DOI 10.1002/(SICI)1097-0134(1999)37:3+<171::AID-PROT21> 3.0.CO
Rohl, C.A., Strauss, C.E.M., Misura, K.M.S., Baker, D., Protein Structure Prediction Using Rosetta (2004) Methods in Enzymology, 383, pp. 66-93. , DOI 10.1016/S0076-6879(04)83004-0
McCammon, J.A., Gelin, B.R., Karplus, M., Dynamics of folded proteins (1977) Nature, 267, pp. 585-590
Metropolis, N., Ulam, S., The Monte Carlo method (1949) J. Am. Stat. Assoc., 44, pp. 335-341
Bradley, P., Malmstrom, L., Qian, B., Schonbrun, J., Chivian, D., Kim, D.E., Meiler, J., Baker, D., Free modeling with Rosetta in CASP6 (2005) Proteins: Structure, Function and Genetics, 61 (SUPPL. 7), pp. 128-134. , DOI 10.1002/prot.20729
Davis, I.W., Leaver-Fay, A., Chen, V.B., Block, J.N., Kapral, G.J., Wang, X., Murray, L.W., Richardson, D.C., MolProbity: All-atom contacts and structure validation for proteins and nucleic acids (2007) Nucleic Acids Res., 35, pp. W375-W383
Wilmot, C.M., Thornton, J.M., β-Turns and their distortions: A proposed new nomenclature (1990) Protein Engineering, 3 (6), pp. 479-493
Pavone, V., Gaeta, G., Lombardi, A., Nastri, F., Maglio, O., Isernia, C., Saviano, M., Discovering protein secondary structures: Classification and description of isolated alphaturns (1996) Biopolymers, 38, pp. 705-721
Rek, A., Brandner, B., Geretti, E., Kungl, A.J., A biophysical insight into the RANTES-glycosaminoglycan interaction (2009) Biochem. Biophys. Acta, 1794, pp. 577-582
Cooper, D.A., Lange, J.M.A., Peptide inhibitors of virus-cell fusion: Enfuvirtide as a case study in clinical discovery and development (2004) Lancet Infectious Diseases, 4 (7), pp. 426-436. , DOI 10.1016/S1473-3099(04)01058-8, PII S1473309904010588
He, Y., Xiao, Y., Song, H., Liang, Q., Ju, D., Chen, X., Lu, H., Zhang, L., Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor (2008) J. Biol. Chem., 283, pp. 11126-11134
Berger, E. A., Murphy, P. M., Farber, J. M., Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease (1999) Annual Review of Immunology, 17, pp. 657-700. , DOI 10. 1146/annurev. immunol. 17. 1. 65
Lederman, M. M., Penn-Nicholson, A., Cho, M., Mosier, D., Biology of CCR5 and its role in HIV infection and treatment (2006) Journal of the American Medical Association, 296 (7), pp. 815-826. , http: //jama. ama-assn. org/cgi/reprint/296/7/815, DOI 10. 1001/jama. 296. 7. 815
Strizki, J. M., Xu, S., Wagner, N. E., Wojcik, L., Liu, J., Hou, Y., Endres, M., Baroudy, B. M., SCH-C (SCH 351125), an orally bioavailable, small molecule antagonist of the chemokine receptor CCR5, is a potent inhibitor of HIV-1 infection in vitro and in vivo (2001) Proceedings of the National Academy of Sciences of the United States of America, 98 (22), pp. 12718-12723. , DOI 10. 1073/pnas. 221375398
Strizki, J. M., Tremblay, C., Xu, S., Wojcik, L., Wagner, N., Gonsiorek, W., Hipkin, R. W., Baroudy, B. M., Discovery and characterization of vicriviroc (SCH 417690), a CCR5 antagonist with potent activity against human immunodeficiency virus type 1 (2005) Antimicrobial Agents and Chemotherapy, 49 (12), pp. 4911-4919. , DOI 10. 1128/AAC. 49. 12. 4911-4919. 2005
Meanwell, N. A., Kadow, J. F., Maraviroc, a chemokine CCR5 receptor antagonist for the treatment of HIV infection and AIDS (2007) Current Opinion in Investigational Drugs, 8 (8), pp. 669-681
Gulick, R. M., Lalezari, J., Goodrich, J., Clumeck, N., DeJesus, E., Horban, A., Nadler, J., Mayer, H., Maraviroc for previously treated patients with R5 HIV-1 infection (2008) N. Engl. J. Med., 359, pp. 1429-1441. , MOTIVATE Study Teams
Skelton, N. J., Aspiras, F., Ogez, J., Schall, T. J., Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type (1995) Biochemistry, 34, pp. 5329-5342
Shaw, J. P., Johnson, Z., Borlat, F., Zwahlen, C., Kungl, A., Roulin, K., Harrenga, A., Proudfoot, A. E. I., The X-ray structure of RANTES: Heparin-derived disaccharides allows the rational design of chemokine inhibitors (2004) Structure, 12 (11), pp. 2081-2093. , DOI 10. 1016/j. str. 2004. 08. 014, PII S0969212604003430
Bax, A. D., Davis, D. G., MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy (1985) J. Magn. Res., 65, pp. 355-360
Hwang, T. L., Shaka, A. J., Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients (1995) J. Magn. Reson. Ser. A, 112, pp. 275-279
Weiner, S. J., Kollman, P. A., Nguyen, D. T., Case, D. A., An all atom force field for simulations of proteins and nucleic acids (1986) J. Comput. Chem., 7, pp. 230-252
Simons, K. T., Bonneau, R., Ruczinski, I., Baker, D., Ab initio protein structure prediction of CASP III targets using ROSETTA (1999) Proteins: Structure, Function and Genetics, 37 (SUPPL. 3), pp. 171-176. , DOI 10. 1002/ (SICI) 1097-0134 (1999) 37: 3+<171:: AID-PROT21> 3. 0. CO
Rohl, C. A., Strauss, C. E. M., Misura, K. M. S., Baker, D., Protein Structure Prediction Using Rosetta (2004) Methods in Enzymology, 383, pp. 66-93. , DOI 10. 1016/S0076-6879 (04) 83004-0
McCammon, J. A., Gelin, B. R., Karplus, M., Dynamics of folded proteins (1977) Nature, 267, pp. 585-590
Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Richardson, D. C., MolProbity: All-atom contacts and structure validation for proteins and nucleic acids (2007) Nucleic Acids Res., 35, pp. W375-W383
Wilmot, C. M., Thornton, J. M., -Turns and their distortions: A proposed new nomenclature (1990) Protein Engineering, 3 (6), pp. 479-493
Cooper, D. A., Lange, J. M. A., Peptide inhibitors of virus-cell fusion: Enfuvirtide as a case study in clinical discovery and development (2004) Lancet Infectious Diseases, 4 (7), pp. 426-436. , DOI 10. 1016/S1473-3099 (04) 01058-8, PII S1473309904010588
Faseb J (ISSN: 0892-6638, 0892-6638linking), 2011 Apr; 25(4): 1230-1243.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.712, 5-year impact factor: 6.34
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79954597305&partnerID=40&md5=b2901bd84e7c3fc1a2ff38f2486ce3d5
Keywords: Aids, Antivirals, Ccr5, Chemokines, Rational Design, Viral Receptors, Chemokine Receptor Ccr5, Chemokine Receptor Cxcr4, Guanine Nucleotide Binding Protein, Rantes, Algorithm, Alpha Helix, Antiviral Activity, Article, Beta 1 Protein Strand, Carboxy Terminal Sequence, Computer Model, Human Immunodeficiency Virus 1, Hydrophobicity, N Loop, Nuclear Magnetic Resonance, Priority Journal, Protein Structure, Amino Acid Sequence, Anti-Hiv Agents, Biomimetic Materials, Chemokine Ccl5, Chemotaxis, Hydrophobic And Hydrophilic Interactions, Biomolecular, P38 Mitogen-Activated Protein Kinases, Peptides, Protein Conformation, Protein Engineering, Signal Transduction, Structure-Activity Relationship,
Affiliations:
*** IBB - CNR ***
Unit of Human Virology, Department of Biological and Technological Research (DIBIT), San Raffaele Scientific Institute, Milan, Italy
Department of Biomedical Sciences, University of Cagliari, Cagliari, Italy
National Research Council (CNR), Istituto di Chimica del Riconoscimento Molecolare (ICRM), Milan, Italy
Department of Chemistry, University of Naples Federico II, Naples, Italy
Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 10 Center Dr., Bethesda, MD 20892, United States
Istituto di Biostrutture e Bioimmagini (IBB), National Research Council (CNR), 80134 Napoli, Italy
References:
Berger, E.A., Murphy, P.M., Farber, J.M., Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease (1999) Annual Review of Immunology, 17, pp. 657-700. , DOI 10.1146/annurev.immunol.17.1.65
Lusso, P., HIV and the chemokine system: 10 years later (2006) EMBO J., 25, pp. 447-456
Lederman, M.M., Penn-Nicholson, A., Cho, M., Mosier, D., Biology of CCR5 and its role in HIV infection and treatment (2006) Journal of the American Medical Association, 296 (7), pp. 815-826. , http://jama.ama-assn.org/cgi/reprint/296/7/815, DOI 10.1001/jama.296.7.815
Strizki, J.M., Xu, S., Wagner, N.E., Wojcik, L., Liu, J., Hou, Y., Endres, M., Baroudy, B.M., SCH-C (SCH 351125), an orally bioavailable, small molecule antagonist of the chemokine receptor CCR5, is a potent inhibitor of HIV-1 infection in vitro and in vivo (2001) Proceedings of the National Academy of Sciences of the United States of America, 98 (22), pp. 12718-12723. , DOI 10.1073/pnas.221375398
Strizki, J.M., Tremblay, C., Xu, S., Wojcik, L., Wagner, N., Gonsiorek, W., Hipkin, R.W., Baroudy, B.M., Discovery and characterization of vicriviroc (SCH 417690), a CCR5 antagonist with potent activity against human immunodeficiency virus type 1 (2005) Antimicrobial Agents and Chemotherapy, 49 (12), pp. 4911-4919. , DOI 10.1128/AAC.49.12.4911-4919.2005
Watson, C., Jenkinson, S., Kazmierski, W., Kenakin, T., The CCR5 receptor-based mechanism of action of 873140, a potent allosteric noncompetitive HIV entry inhibitor (2005) Molecular Pharmacology, 67 (4), pp. 1268-1282. , DOI 10.1124/mol.104.008565
Meanwell, N.A., Kadow, J.F., Maraviroc, a chemokine CCR5 receptor antagonist for the treatment of HIV infection and AIDS (2007) Current Opinion in Investigational Drugs, 8 (8), pp. 669-681
Gulick, R.M., Lalezari, J., Goodrich, J., Clumeck, N., DeJesus, E., Horban, A., Nadler, J., Mayer, H., Maraviroc for previously treated patients with R5 HIV-1 infection (2008) N. Engl. J. Med., 359, pp. 1429-1441. , MOTIVATE Study Teams
Nardese, V., Longhi, R., Polo, S., Sironi, F., Arcelloni, C., Paroni, R., Desantis, C., Lusso, P., Structural determinants of CCR5 recognition and HIV-1 blockade in RANTES (2001) Nature Structural Biology, 8 (7), pp. 611-615. , DOI 10.1038/89653
Vangelista, L., Longhi, R., Sironi, F., Pavone, V., Lusso, P., Critical role of the N-loop and β1-strand hydrophobic clusters of RANTES-derived peptides in anti-HIV activity (2006) Biochemical and Biophysical Research Communications, 351 (3), pp. 664-668. , DOI 10.1016/j.bbrc.2006.10.090, PII S0006291X06023321
Skelton, N.J., Aspiras, F., Ogez, J., Schall, T.J., Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type (1995) Biochemistry, 34, pp. 5329-5342
Chung, C., Cooke, R.M., Proudfoot, A.E., Wells, T.N.C., The three-dimensional solution structure of RANTES (1995) Biochemistry, 34, pp. 9307-9314
Wilken, J., Hoover, D., Thompson, D.A., Barlow, P.N., McSparron, H., Picard, L., Wlodawer, A., Kent, S.B.H., Total chemical synthesis and high-resolution crystal structure of the potent anti-HIV protein AOP-RANTES (1999) Chemistry and Biology, 6 (1), pp. 43-51. , DOI 10.1016/S1074-5521(99)80019-2
Shaw, J.P., Johnson, Z., Borlat, F., Zwahlen, C., Kungl, A., Roulin, K., Harrenga, A., Proudfoot, A.E.I., The X-ray structure of RANTES: Heparin-derived disaccharides allows the rational design of chemokine inhibitors (2004) Structure, 12 (11), pp. 2081-2093. , DOI 10.1016/j.str.2004.08.014, PII S0969212604003430
Nussbaum, O., Broder, C.C., Berger, E.A., Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation (1994) Journal of Virology, 68 (9), pp. 5411-5422
Lusso, P., Cocchi, F., Balotta, C., Markham, P.D., Louie, A., Farci, P., Pal, R., Reitz Jr., M.S., Growth of macrophage-tropic and primary human immunodeficiency virus type 1 (HIV-1) isolates in a unique CD4 + T-cell clone (PM1): Failure to downregulate CD4 and to interfere with cell-line-tropic HIV-1 (1995) J. Virol., 69, pp. 3712-3720
Bax, A.D., Davis, D.G., MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy (1985) J. Magn. Res., 65, pp. 355-360
Jeener, J., Meier, B.H., Bachmann, P., Ernst, R.R., Investigation of exchange processes by two-dimensional NMR spectroscopy (1979) J. Chem. Phys., 71, pp. 4546-4553
Kumar, A., Wagner, G., Ernst, R.R., Wuthrich, K., Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy implications for studies of protein conformation (1981) J. Am. Chem. Soc., 103, pp. 3654-3658
Griesinger, C., Ernst, R.R., Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy (1978) Ø Magn. Res., 75, pp. 261-271
Piantini, U., Srensen, O.W., Ernst, R.R., Multiple quantum filters for elucidating NMR coupling networks (1982) J. Am. Chem. Soc., 104, pp. 6800-6801
Wuthrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley, New York
Marion, D., Wuthrich, K., Application of phase sensitive correlated spectroscopy (COSY) for measurements of proton-proton spin-spin coupling constants in proteins (1983) Biochem. Biophys. Res. Commun., 113, pp. 967-974
Hwang, T.L., Shaka, A.J., Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients (1995) J. Magn. Reson. Ser. A, 112, pp. 275-279
Keller, R., (2004) The Computer Aided Resonance Assignment Tutorial, , www.nmr.ch, ISBN 3-85600-112-3, CANTINA Verlag available from
Guntert, P., Braun, W., Wuthrich, K., Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA (1991) Journal of Molecular Biology, 217 (3), pp. 517-530
Guntert, P., Mumenthaler, C., Wuthrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) Journal of Molecular Biology, 273 (1), pp. 283-298. , DOI 10.1006/jmbi.1997.1284
Weiner Scott, J., Kollman Peter, A., Case David, A., Singh U.Chandra, Alagona Giuliano, Profeta Jr. Salvatore, Weiner Paul, Ghio Caterina, NEW FORCE FIELD FOR MOLECULAR MECHANICAL SIMULATION OF NUCLEIC ACIDS AND PROTEINS. (1984) Journal of the American Chemical Society, 106 (3), pp. 765-784
Weiner, S.J., Kollman, P.A., Nguyen, D.T., Case, D.A., An all atom force field for simulations of proteins and nucleic acids (1986) J. Comput. Chem., 7, pp. 230-252
Simons, K.T., Bonneau, R., Ruczinski, I., Baker, D., Ab initio protein structure prediction of CASP III targets using ROSETTA (1999) Proteins: Structure, Function and Genetics, 37 (SUPPL. 3), pp. 171-176. , DOI 10.1002/(SICI)1097-0134(1999)37:3+<171::AID-PROT21> 3.0.CO
Rohl, C.A., Strauss, C.E.M., Misura, K.M.S., Baker, D., Protein Structure Prediction Using Rosetta (2004) Methods in Enzymology, 383, pp. 66-93. , DOI 10.1016/S0076-6879(04)83004-0
McCammon, J.A., Gelin, B.R., Karplus, M., Dynamics of folded proteins (1977) Nature, 267, pp. 585-590
Metropolis, N., Ulam, S., The Monte Carlo method (1949) J. Am. Stat. Assoc., 44, pp. 335-341
Bradley, P., Malmstrom, L., Qian, B., Schonbrun, J., Chivian, D., Kim, D.E., Meiler, J., Baker, D., Free modeling with Rosetta in CASP6 (2005) Proteins: Structure, Function and Genetics, 61 (SUPPL. 7), pp. 128-134. , DOI 10.1002/prot.20729
Davis, I.W., Leaver-Fay, A., Chen, V.B., Block, J.N., Kapral, G.J., Wang, X., Murray, L.W., Richardson, D.C., MolProbity: All-atom contacts and structure validation for proteins and nucleic acids (2007) Nucleic Acids Res., 35, pp. W375-W383
Wilmot, C.M., Thornton, J.M., β-Turns and their distortions: A proposed new nomenclature (1990) Protein Engineering, 3 (6), pp. 479-493
Pavone, V., Gaeta, G., Lombardi, A., Nastri, F., Maglio, O., Isernia, C., Saviano, M., Discovering protein secondary structures: Classification and description of isolated alphaturns (1996) Biopolymers, 38, pp. 705-721
Rek, A., Brandner, B., Geretti, E., Kungl, A.J., A biophysical insight into the RANTES-glycosaminoglycan interaction (2009) Biochem. Biophys. Acta, 1794, pp. 577-582
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Molecular engineering of RANTES peptide mimetics with potent anti-HIV-1 activity
The chemokine receptor CCR5 is utilized as a critical coreceptor by most primary HIV-1 strains. While the lack of structural information on CCR5 has hampered the rational design of specific inhibitors, mimetics of the chemokines that naturally bind CCR5 can be molecularly engineered. We used a structure-guided approach to design peptide mimetics of the N-loop and beta 1-strand regions of regulated on activation normal T-cell-expressed and secreted (RANTES)/CCL5, which contain the primary molecular determinants of HIV-1 blockade. Rational modifications were sequentially introduced into the N-loop/beta 1-strand sequence, leading to the generation of mimetics with potent activity against a broad spectrum of CCR5-specific HIV-1 isolates (IC(50) range: 104-640 nM) but lacking activity against CXCR4-specific HIV-1 isolates. Functional enhancement was initially achieved with the stabilization of the N loop in the beta-extended conformation adopted in full-length RANTES, as confirmed by nuclear magnetic resonance (NMR) analysis. However, the most dramatic increase in antiviral potency resulted from the engraftment of an in silico-optimized linker segment designed using de novo structure-prediction algorithms to stabilize the C-terminal alpha-helix and experimentally validated by NMR. Our mimetics exerted CCR5-antagonistic effects, demonstrating that the antiviral and proinflammatory functions of RANTES can be uncoupled. RANTES peptide mimetics provide new leads for the development of safe and effective HIV-1 entry inhibitors.-Lusso, P., Vangelista, L., Cimbro, R., Secchi, M., Sironi, F., Longhi, R., Faiella, M., Maglio, O., Pavone, V. Molecular engineering of RANTES peptide mimetics with potent anti-HIV-1 activity. FASEB J. 25, 1230-1243 (2011). www.fasebj.org
The chemokine receptor CCR5 is utilized as a critical coreceptor by most primary HIV-1 strains. While the lack of structural information on CCR5 has hampered the rational design of specific inhibitors, mimetics of the chemokines that naturally bind CCR5 can be molecularly engineered. We used a structure-guided approach to design peptide mimetics of the N-loop and beta 1-strand regions of regulated on activation normal T-cell-expressed and secreted (RANTES)/CCL5, which contain the primary molecular determinants of HIV-1 blockade. Rational modifications were sequentially introduced into the N-loop/beta 1-strand sequence, leading to the generation of mimetics with potent activity against a broad spectrum of CCR5-specific HIV-1 isolates (IC(50) range: 104-640 nM) but lacking activity against CXCR4-specific HIV-1 isolates. Functional enhancement was initially achieved with the stabilization of the N loop in the beta-extended conformation adopted in full-length RANTES, as confirmed by nuclear magnetic resonance (NMR) analysis. However, the most dramatic increase in antiviral potency resulted from the engraftment of an in silico-optimized linker segment designed using de novo structure-prediction algorithms to stabilize the C-terminal alpha-helix and experimentally validated by NMR. Our mimetics exerted CCR5-antagonistic effects, demonstrating that the antiviral and proinflammatory functions of RANTES can be uncoupled. RANTES peptide mimetics provide new leads for the development of safe and effective HIV-1 entry inhibitors.-Lusso, P., Vangelista, L., Cimbro, R., Secchi, M., Sironi, F., Longhi, R., Faiella, M., Maglio, O., Pavone, V. Molecular engineering of RANTES peptide mimetics with potent anti-HIV-1 activity. FASEB J. 25, 1230-1243 (2011). www.fasebj.org
Molecular engineering of RANTES peptide mimetics with potent anti-HIV-1 activity
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Molecular engineering of RANTES peptide mimetics with potent anti-HIV-1 activity
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Ronda L, Tonelli A, Sogne E, Autiero I, Spyrakis F, Pellegrino S, Abbiati G, Maffioli E, Schulte C, Piano R, Cozzini P, Mozzarelli A, Bettati S, Clerici F, Milani P, Lenardi C, Tedeschi G, Gelmi ML
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Impact Factor: 3.275
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Caserta G, Chino M, Firpo V, Zambrano G, Leone L, D'Alonzo D, Nastri F, Maglio O, Pavone V, Lombardi A
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Cucciolito ME, Trinchillo M, Iannitti R, Palumbo R, Tesauro D, Tuzi A, Ruffo F, D'Amora A
* Sugar-Incorporated N-Heterocyclic-Carbene-Containing Gold(I) Complexes: Synthesis, Characterization, and Cytotoxic Evaluation (328 views)
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Pacifico F, Lepore A, Mellone S, Sanguigno L, Federico G, Greco A, Brunetti A, Leonardi A
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D'Ambrosio K, Lopez M, Dathan NA, Ouahrani-bettache S, Köhler S, Ascione G, Monti SM, Winum JY, De Simone G
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Cantisani M, Vitiello M, Falanga A, Finamore E, Galdiero M, Galdiero S
* Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity (510 views)
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Yonath A, Bashan A, Zarivach R, Franceschi F, Schluenzen F, Harms J, Albrecht R, Berisio R
* Methods Of Growing Crystals Of Free, Antibiotic-Complexed, And Substrate-Complexed Large Ribosomal Subunits, And Methods Of Rational Designing Or Identifying Antibiotics Using Structure Coordinate Data Derived From Such Crystals (292 views)
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* Rational Design of a User-Friendly Aptamer/Peptide-Based Device for the Detection of Staphylococcus aureus (84 views)
Sensors (ISSN: 1424-8220linking, 1424-3210), 2020 Sep 2; 20(17): N/D-N/D.
Impact Factor: 3.275
View Export to BibTeX Export to EndNote
Caserta G, Chino M, Firpo V, Zambrano G, Leone L, D'Alonzo D, Nastri F, Maglio O, Pavone V, Lombardi A
* Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design (266 views)
Chembiochem, 2018; 19: 1823-1826.
Impact Factor: 2.774
View Export to BibTeX Export to EndNote
Cucciolito ME, Trinchillo M, Iannitti R, Palumbo R, Tesauro D, Tuzi A, Ruffo F, D'Amora A
* Sugar-Incorporated N-Heterocyclic-Carbene-Containing Gold(I) Complexes: Synthesis, Characterization, and Cytotoxic Evaluation (328 views)
Eur J Inorg Chem (ISSN: 1434-1948, 1099-0682e), 2017; 2017(42): 4855-4961.
Impact Factor: 2.507
View Export to BibTeX Export to EndNote
Pacifico F, Lepore A, Mellone S, Sanguigno L, Federico G, Greco A, Brunetti A, Leonardi A
* The chemokine scavenging receptor D6/ACKR2 is a target of miR-146a in thyroid cancer (145 views)
Genes Cancer (ISSN: 1947-6019), 2017; 8(5-6): 577-588.
Impact Factor: 0
View Export to BibTeX Export to EndNote
D'Ambrosio K, Lopez M, Dathan NA, Ouahrani-bettache S, Köhler S, Ascione G, Monti SM, Winum JY, De Simone G
* Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis (453 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 0300-9084linking), 2014 Feb; 97(1): 114-120.
Impact Factor: 2.963
View Export to BibTeX Export to EndNote
Cantisani M, Vitiello M, Falanga A, Finamore E, Galdiero M, Galdiero S
* Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity (510 views)
Int J Nanomed (ISSN: 1178-2013, 1176-9114, 1178-2013electronic), 2012; 7: 2361-2371.
Impact Factor: 3.463
View Export to BibTeX Export to EndNote
Yonath A, Bashan A, Zarivach R, Franceschi F, Schluenzen F, Harms J, Albrecht R, Berisio R
* Methods Of Growing Crystals Of Free, Antibiotic-Complexed, And Substrate-Complexed Large Ribosomal Subunits, And Methods Of Rational Designing Or Identifying Antibiotics Using Structure Coordinate Data Derived From Such Crystals (292 views)
International Publication Number, 2003; N/D: N/D-N/D.
Impact Factor: 4.622
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7 Records (7 excluding Abstracts).
Total impact factor: 19.604 (19.604 excluding Abstracts).
Total 5 year impact factor: 17.135 (17.135 excluding Abstracts).
Total impact factor: 19.604 (19.604 excluding Abstracts).
Total 5 year impact factor: 17.135 (17.135 excluding Abstracts).
568 views. Last view on Saturday 14 January 2023, 20:03:26
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