Synthesis and structural characterization of the ligand binding site of macrophage scavenger receptor

The macrophage scavenger receptor (SR) mediates the endocytosis of modified LDLs. These ligands, when incorporated in excess, promote the conversion of macrophages into foam cells, which may result in arterial sclerosis. The modified LDL-binding site in human SR is located in the collagen-like domain (HSR(323-341): Ala-Gly-Arg-Pro-Gly-Asn-SerGly-Pro-Lys-Gly-Gln-Lys-Gly-Glu-Lys-Gly-Ser-Gly) [1]. In the present study, a new synthetic strategy for trimeric peptides was developed and applied to the syntheses of HSR(323-341) models (Fig. 1). The effect of spacer (X) on the structure was characterized by CD.