Synthesis and Conformational Studies of Novel, Side-Chain Protected, L-(αMe)Ser Homo-Peptides

摘要

In search for new, conformationally constrained, amino acid residues endowed with potentially interesting features, we started a research programme aimed at investigating the physico-chemical properties of (αMe)Ser-rich peptides. In addition to the 3D-structural peculiarities of C~(α,α)-disubstituted glycines, (αMe)Ser is expected to impart valuable solubility and biological (e.g., serine protease-like) properties when inserted into appropriately designed peptides. In the first step of this programme we synthesized and investigated the preferred conformation of the terminally- and side-chain blocked L-(αMe)Ser(Bzl) homo-peptides to the hexamer level shown below.