Premium
Recognition in cell adhesion. A comparative study of the conformations of RGD‐containing peptides by Monte Carlo and NMR methods
Author(s) -
Cachau Raul E.,
Serpersu Engin H.,
Mildvan Albert S.,
August J. Thomas,
Amzel L. Mario
Publication year - 1989
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300020407
Subject(s) - chemistry , vitronectin , pentapeptide repeat , cell adhesion , fibronectin , monte carlo method , nuclear magnetic resonance spectroscopy , sequence (biology) , peptide , adhesion , biophysics , stereochemistry , biochemistry , cell , organic chemistry , biology , statistics , mathematics
Many of the proteins that mediate cell adhesion processes–fibronectin, fibrinogen, vitronectin, von Willebrand factor, osteopontin, laminin and various collagens – contain the amino acid sequence Arg‐Gly‐Asp. Short peptides that include this sequence have been shown to inhibit the interactions of cell adhesion proteins with their receptors and to have dramatic effects on developmental processes involving cellular recognition. In order to determine which conformations are accessible to Arg‐Gly‐Asp containing peptides, we analyzed tri‐, tetra‐ and pentapeptide using molecular mechanics and Monte Carlo methods, and studied the solution conformations of the pentapeptide Gly‐Arg‐Gly‐Asp‐Ser using nuclear magnectic resonance techniques. The Monte Carlo method was used to: (a) identify the low energy conformations of the peptides and (b) evaluate their thermodynamic properties. In the case of the pentapeptide Gly‐Arg‐Gly‐Asp‐Gly, the four stable conformations include three with reverse turns and one open structure. The conformations found in this analysis are compatible with the nuclear magnetic resonance (nuclear Overhauser effect) data.