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A synthetic model of collagen structure taken from bovine macrophage scavenger receptor
Author(s) -
Tanaka Toshiki,
Wada Yayoi,
Nakamura Haruki,
Doi Takefumi,
Imanishi Takeshi,
Kodama Tatsuhiko
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80693-o
Subject(s) - scavenger receptor , macrophage , chemistry , scavenger , receptor , microbiology and biotechnology , biophysics , biochemistry , biology , in vitro , radical , lipoprotein , cholesterol
A putative collagen structure from macrophage scavenger receptors binds to a wide range of ligands. In order to elucidate the ligand's binding mode, this collagen structure was constructed using short peptides. This was accomplished by the reaction of a tri‐bromoacetylated branched peptide with a purified unprotected 25‐residue peptide, which contained Cys, 4 repeats of the triplet, Gly‐Pro‐Hyp, and 12 residues from the bovine macrophage scavenger receptor (residues 332 to 343). The three identical 25‐residue peptides are linked at the N‐terminus. CD and NMR spectra of the N‐terminus cross‐linked tripeptide show that it forms a collagen structure below 10°C and an extended structure at high temperature with a midpoint of 20° C.