Conformational Analysis Of Novel Heparin Binding Peptides

Conformational Analysis Of Novel Heparin Binding Peptides (231 visite)

Vacatello M, D'Auria G, Falcigno L, Dettin M, Gambaretto R, Di Bello C, Paolillo L

Biomaterials (ISSN: 0142-9612, 1878-5905electronic), 2005 Jun; 26(16): 3207-3214.

Tipo di articolo: Journal Article,

Impact factor: 4.698, Impact factor a 5 anni: 8.911

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-10644256415&partnerID=40&md5=491682c15a895942245788b302474699

Parole chiave: Amino Acid Sequence, Biocompatible Materials Chemistry, Cell Adhesion, Circular Dichroism, Heparin Chemistry, Humans, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Osteoblasts Cytology Metabolism, Peptides Chemistry, Polystyrenes Chemistry, Protein Conformation, Proteoglycans Chemistry, Protons, Software, Tissue Engineering Methods, Vitronectin Chemistry, Ionic Interactions, Biomedical Engineering, Computer Simulation, Dentistry, Molecular Structure, Polypeptides, Biomaterials, Heparin Binding Protein, Methionylalanylprolylarginylprolylserylleucylalanyllysyllysylglutaminyl Arginylphenylalanylarginylhistidylarginylasparaginylarginyllysylglycyltyrosyl Arginylserylglutaminylarginylglycine, Peptide Derivative, Unclassified Drug, Adsorption, Analytic Method, Article, Binding Site, Electricity, Hydrophobicity, Molecular Model, Nuclear Magnetic Resonance, Priority Journal, Protein Analysis, Protein Localization, Protein Protein Interaction, Protein Structure, Sequence Analysis, Structure Analysis, Surface Property,

Affiliazioni:

*** IBB - CNR ***
Department of Chemistry, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, via Cintia-80126 Naples, Italy. manuela@chemistry.unina.it
Inst. of Biostructure and Bioimaging, CNR, Via Mezzocannone 6-80134 Naples, I., Italy
Dept. of Chem. Process Engineering, University of Padua, Via Marzolo 9, 35131 Padua, Italy, Italy

Riferimenti:

Anselme, K., Osteoblast adhesion on biomaterials (2000) Biomaterials, 21, pp. 667-68

Puleo, D.A., Bizios, R., RGDS tetrapeptide binds to osteoblasts and inhibits fibronectin-mediated adhesion (1991) Bone, 12 (4), pp. 271-276

Dalton, B.A., McFarland, C.D., Underwood, P.A., Steele, J.G., Role of the heparin binding domain of fibronectin in attachment and spreading of human bone-derived cells (1995) J Cell Sci, 108, pp. 2083-2092

Cardin, A.D., Weintraub, H.J., Molecular modeling of protein-glycosaminoglycan interactions (1989) Arteriosclerosis, 9 (1), pp. 21-32

Lin, H.B., Sun, W., Mosher, D.F., Garcia-Echeverria, C., Schaufelberger, K., Lelkes, P.I., Cooper, S.L., Synthesis, surface, and cell-adhesion properties of polyurethanes containing covalently grafted RGD-peptides (1994) J Biomed Mater Res, 28 (3), pp. 329-342

Rezania, A., Healy, K.E., Biomimetic peptide surfaces that regulate adhesion, spreading, cytoskeletal organization, and mineralization of the matrix deposited by osteoblast-like cells (1999) Biotechnol Prog, 15 (1), pp. 19-32

Dettin, M., Conconi, M.T., Gambaretto, R., Pasquato, A., Folin, M., Di Bello, C., Parnigotto, P.P., Novel osteoblast-adhesive peptides for dental/orthopedic biomaterials (2002) J Biomed Mater Res, 60, pp. 466-471

Chon, J.H., Chaikof, E.L., Soluble heparin-binding peptides regulate chemokinesis and cell adhesive forces (2001) Am J Physiol Cell Physiol, 280 (6), pp. C1394-C1402

Mulloy, B., Forster, M.J., Jones, C., Davies, D.B., N.m.r. and molecular-modelling studies of the solution conformation of heparin (1993) Biochem J, 293, pp. 849-858

Bax, A.D., Davis, D.G., MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy (1985) J Magn Res, 65 (2), pp. 355-360

Jeener, J., Meier, B.H., Bachmann, P., Ernst, R.R.J., Investigation of exchange processes by two-dimensional NMR spectroscopy (1979) Chem Phys, 71, pp. 4546-4553

Kumar, A., Wagner, G., Ernst, R.R., Wuethrich, 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 (13), pp. 3654-3658

Piantini, U., Sørensen, O.W., Ernst, R.R., Multiple quantum filters for elucidating NMR coupling networks (1982) J Am Chem Soc, 104 (24), pp. 6800-6801

Wüthrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley New York

Johnson, B.A., Blevins, R.A., NMRView: A computer program for the visualization and analysis of NMR data J Biomol NMR, 4, pp. 603-614

Guntert, P., Mumenthaler, C., Wuethrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) J Mol Biol, 273 (1), pp. 283-298

Wuethrich, K., Billeter, M., Braun, W., Pseudostructures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance (1983) J Mol Biol, 169 (4), pp. 949-961

Guntert, P., Wuthrich, K., Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints (1991) J Biomol NMR, 1 (4), pp. 447-456

Case, D.A., Pearlman, D.A., Caldwell, J.W., Cheatham III, T.E., Ross, W.S., Simmerling, C.L., Darden, T.A., Kollman, P.A., (1996) AMBER 6, , University of California, San Francisco

Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham, T.E.I.I.I., Debolt, S., Ferguson, D., Kollman, P., AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to stimulate the structural and energetic properties of molecules (1995) Comp Phys Commun, 91 (13), pp. 1-42

Weiner, S.J., Kollmann, P.A., Nguyen, D.T., Case, D.A., An all atom forcefield for simulations of proteins and nucleic acids (1986) J Comput Chem, 7 (2), pp. 230-252

Koradi, R., Billeter, M., Wuethrich, K., MOLMOL: A program for display and analysis of macromolecular structures (1996) J Mol Graphics, 14 (1), pp. 51-55

Lifson, S., Hagler, A.T., Dauber, P., Consistent force field studies of intermolecular forces in hydrogen-bonded crystals. 1. Carboxylic acids, amides, and the C:O...H- hydrogen bonds (1979) J Am Chem Soc, 101 (18), pp. 5111-5121

Fletcher, R., Reeves, C.M., Function minimization by conjugate gradients (1964) Comput J, 7, pp. 149-154

Van Gunsteren, W.F., Karplus, M., A method for constrained energy minimization of macromolecules (1980) J Comput Chem, 1 (3), pp. 266-274

Brooks III, C.L., Montgomery Pettitt, B., Karplus, M., (1988) Proteins: A Theoretical Perspective of Dynamics, Structure and Thermodynamics. Advances in Chemical Physics, 71. , Wiley New York

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 (2), pp. 311-333

Puleo, D. A., Bizios, R., RGDS tetrapeptide binds to osteoblasts and inhibits fibronectin-mediated adhesion (1991) Bone, 12 (4), pp. 271-276

Dalton, B. A., McFarland, C. D., Underwood, P. A., Steele, J. G., Role of the heparin binding domain of fibronectin in attachment and spreading of human bone-derived cells (1995) J Cell Sci, 108, pp. 2083-2092

Cardin, A. D., Weintraub, H. J., Molecular modeling of protein-glycosaminoglycan interactions (1989) Arteriosclerosis, 9 (1), pp. 21-32

Lin, H. B., Sun, W., Mosher, D. F., Garcia-Echeverria, C., Schaufelberger, K., Lelkes, P. I., Cooper, S. L., Synthesis, surface, and cell-adhesion properties of polyurethanes containing covalently grafted RGD-peptides (1994) J Biomed Mater Res, 28 (3), pp. 329-342

Chon, J. H., Chaikof, E. L., Soluble heparin-binding peptides regulate chemokinesis and cell adhesive forces (2001) Am J Physiol Cell Physiol, 280 (6), pp. C1394-C1402

Bax, A. D., Davis, D. G., MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy (1985) J Magn Res, 65 (2), pp. 355-360

Piantini, U., S rensen, O. W., Ernst, R. R., Multiple quantum filters for elucidating NMR coupling networks (1982) J Am Chem Soc, 104 (24), pp. 6800-6801

W thrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley New York

Johnson, B. A., Blevins, R. A., NMRView: A computer program for the visualization and analysis of NMR data J Biomol NMR, 4, pp. 603-614

Case, D. A., Pearlman, D. A., Caldwell, J. W., Cheatham III, T. E., Ross, W. S., Simmerling, C. L., Darden, T. A., Kollman, P. A., (1996) AMBER 6, , University of California, San Francisco

Pearlman, D. A., Case, D. A., Caldwell, J. W., Ross, W. S., Cheatham, T. E. I. I. I., Debolt, S., Ferguson, D., Kollman, P., AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to stimulate the structural and energetic properties of molecules (1995) Comp Phys Commun, 91 (13), pp. 1-42

Weiner, S. J., Kollmann, P. A., Nguyen, D. T., Case, D. A., An all atom forcefield for simulations of proteins and nucleic acids (1986) J Comput Chem, 7 (2), pp. 230-252

Van Gunsteren, W. F., Karplus, M., A method for constrained energy minimization of macromolecules (1980) J Comput Chem, 1 (3), pp. 266-274

Brooks III, C. L., Montgomery Pettitt, B., Karplus, M., (1988) Proteins: A Theoretical Perspective of Dynamics, Structure and Thermodynamics. Advances in Chemical Physics, 71. , Wiley New York

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 (2), pp. 311-333

A properly engineered biomaterial for dental/orthopaedic applications must induce specific responses from the osteoblasts at the implant site. A most desirable response is an efficient adhesion, as it represents the first phase in the cell/material interaction and the quality of this phase will influence the cell's capacity to organize into a new functional tissue. The four osteoblast-adhesive peptides discussed in this paper are mapped on the 339-364 sequence ((339) MAPRPSLAKKQRFRHRNRKGYRSQRG (364)) located in the primary heparin-binding site of human vitronectin (HVP). Adsorbed on a polystyrene scaffold, these peptides display different adhesive activities towards osteoblasts. In this paper we report on the structural analysis in solution of the peptides through NMR and computational techniques. We find that the peptides with the highest adhesive activities display a hydrophobic patch opposite to the charged surface candidate to interact with heparin. These findings suggest that the peptides might adsorb on the polystyrene support in a favourable orientation for their activity. Furthermore, molecular models obtained for the four peptides in solution were used in rigid docking simulations with a heparin model. Assuming that the peptide solution conformations are not very different from the polystyrene-adsorbed structures, the simulations reveal that peptide adhesive activity is also affected by the number of ionic interactions and spacing between charged residues. (C) 2004 Elsevier Ltd. All rights reserved