TY - JOUR
T1 - Recognition in cell adhesion. A comparative study of the conformations of RGD‐containing peptides by Monte Carlo and NMR methods
AU - Cachau, Raul E.
AU - Serpersu, Engin H.
AU - Mildvan, Albert S.
AU - August, J. Thomas
AU - Amzel, L. Mario
PY - 1989/12
Y1 - 1989/12
N2 - 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.
AB - 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.
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U2 - 10.1002/jmr.300020407
DO - 10.1002/jmr.300020407
M3 - Article
C2 - 2637044
AN - SCOPUS:0024781710
SN - 0952-3499
VL - 2
SP - 179
EP - 186
JO - Journal of Molecular Recognition
JF - Journal of Molecular Recognition
IS - 4
ER -