Dynamic Forcing, a Method for Evaluating Activity and Selectivity Profiles of RGD (Arg‐Gly‐Asp) Peptides

The easy interconversion between two conformations, which is deduced from molecular dynamics simulations, explains why the cyclopeptide 1 is equally well bound to two receptors whereas the very similar cyclopeptide 2 shows a selectivity towards these receptors of ca. 30:1. The method of “dynamic forcing” showed that 1 can very easily be transformed from its most stable conformation into a conformation which corresponds to that of 2. Thus, for the first time a connection between the biological activity of a compound and its conformational freedom has been established. (Formula Presented.)