Abstract

Formylpeptide receptors are well-characterized receptors which participate in host defense responses of neutrophils. We designed and synthesized chemotactic peptide analog with pbenzoylphenylalanine (Bpa) and biotin to probe structural and mechanistic aspects of peptide-receptor interaction. These peptides possess biological activities which were dependent upon spacer residue length of and Bpa position. The covalent photoaffinity label was detected by Streptavidine-blot, which was inhibited by the parent peptide.

Keywords: chemotactic peptide, fmlp, formylpeptide receptor, photoaffinity labeling, cross-linking, p-benzoylphenylalanine, affinity tag, biotin