Key result
NMR and molecular dynamics simulations revealed that the cyclic RGD peptide exhibits a major conformer with a distorted type II beta-turn and a minor conformer with a turn-extended-turn.
Structural analysis of a cyclic RGD peptide highlights the importance of a hydrophobic residue adjacent to the RGD sequence for selective GPIIb/IIIa receptor binding.
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Cautions against clinical translation of cyclic RGD peptides; leaves open whether conformational features enhance GPIIb/IIIa selectivity in vivo.
Jois et al. (1996) studied this question. cyclo(2,10)Ac-Gly1-Pen2-Gly3-His4-Arg5-Gly6-Asp7-Leu8-Arg9-Cys10-Ala11-NH2 (1) was evaluated on Peptide conformation in solution. NMR and molecular dynamics simulations revealed that the cyclic RGD peptide exhibits a major conformer with a distorted type II beta-turn and a minor conformer with a turn-extended-turn.
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