SYNTHESIS AND STRUCTURAL CHARACTERIZATION OF TRIPLE-HELICAL PEPTIDES WHICH MIMIC THE LIGAND-BINDING SITE OF THE HUMAN MACROPHAGE SCAVENGER RECEPTOR

A synthetic method for triple-helical peptides was developed. Peptides with and without glutamic acid alpha-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 ac tivation of the thioester group by silver ions. This method was applie d to the synthesis of model peptides, which mimic the binding site of. modified low density lipoprotein (LDL) in the human scavenger recepto r (SR). These models possessed different spacers, which connect the pe ptide chains and the crosslinking site. CD and DSC analysis of the pep tides revealed that spacer length has a critical effect on the stabili ty of the triple helix. (C) 1997 Elsevier Science Ltd.