Conformational Analysis Of Novel Heparin Binding Peptides(473 views visite) Vacatello M, D'Auria G, Falcigno L, Dettin M, Gambaretto R, Di Bello C, Paolillo L
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
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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
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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
Conformational Analysis Of Novel Heparin Binding Peptides
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
Conformational Analysis Of Novel Heparin Binding Peptides
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