Beta-Turns are known to be common structural motifs comprising up to 25% of all residues in folded proteins and peptides. Beta-Turns also appear to play important roles in stabilizing tertiary structures, initiating folding and facilitating intramolecular recognition. Recently, as a part of our research work toward the synthesis of new small constrained mimetics of turn structure, we have described solution reactions to produce beta-turn mimetics based on thiazolidine moiety (structure A, Fig. 1). In this communication we report the synthesis of two small libraries of beta-turn mimetics in solid phase (Al and A2) and the conformational analysis by molecular modeling of a model peptide.
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