Preferred conformations of a linear RGD tripeptide.
Conformational study of RGD tripeptides in the nonhydrated and hydrated states was carried out using an empirical potential function ECEPP/3 and the hydration shell model in order to investigate preferred conformations and factors responsible for their stability. RGD tripeptides in the nonhydrated and hydrated states can be interpreted as existing as an ensemble of feasible conformations rather than as a single dominant conformation from the analysis of distributions of backbone conformations, hydrogen bonds and beta-turns. The different distributions of conformations for the neutral and zwitterionic RGD tripeptides in both states may indicate that the conformation of the RGD tripeptide is liable to depend on solvent polarity and pH values. beta-Turn populations for the neutral tripeptide in both states are reasonably consistent with NMR measurements on linear RGD-containing peptides. The degradation of RGD tripeptide seems to be attributed mainly to the hydrogen bonds between the Asp side-chain and the backbone of Asp residue or C-terminal NHMe group, rather than to the flexible backbones of Gly and Asp residues.
Kang
Y K
YK
Department of Chemistry, Chungbuk National University, Cheongju, Korea. ykkang@cbucc.chungbuk.ac.kr
Jhon
J S
JS
D001224:Aspartic Acid / Q000737:chemistry; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides / Q000737:chemistry*; D010452:Peptide Biosynthesis; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013816:Thermodynamics; D014867:Water / Q000378:metabolism
D009842:Oligopeptides; D014867:Water; D001224:Aspartic Acid; C047981:arginyl-glycyl-aspartic acid