Synthesis and structural characterization of triple-helical peptides which mimic the ligand binding site of the human macrophage scavenger receptor

Abstract

A synthetic method for triple-helical peptides was developed. Peptides with and without glutamic acid α-thioester at their N-termini are prepared by the solid-phase method. These peptides are crosslinked at their N-termini one by one to generate trimeric peptides using the activation of the thioester group by silver ions. This method was applied to the synthesis of model peptides, which mimic the binding site of modified low density lipoprotein (LDL) in the human scavenger receptor (SR). These models possessed different spacers, which connect the peptide chains and the crosslinking site. CD and DSC analysis of the peptides revealed that spacer length has a critical effect on the stability of the triple helix.