title: Understanding Lipid Recognition by Protein-Mimicking Cyclic Peptides.
abstract: This paper describes our investigation of the structural determinants of a designed cyclic peptide (cLac, cyclic peptide mimicking lactadherin)1for phosphatidylserine (PS) recognition. A highly efficient strategy that takes advantage of the native chemical ligation (NCL) chemistry has been developed for the synthesis and labeling of cyclic peptides in general. Ala scanning of the cLac peptide revealed a sophisticated model for PS binding, in which the peptide scaffold assembles multiple polar residues to balance the desolvation and electrostatic interactions (salt bridge and hydrogen bonding) to achieve lipid selectivity. The results suggest that cLac effectively mimics the membrane binding mechanism of the parent protein lactadherin.
authors.affiliation: Department of Chemistry, Merkert Chemistry Center, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467.
authors.forename: Azade S
authors.initials: AS
authors.lastname: Hosseini
authors.affiliation: Department of Chemistry, Merkert Chemistry Center, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467.
authors.forename: Hong
authors.initials: H
authors.lastname: Zheng
authors.affiliation: Department of Chemistry, Merkert Chemistry Center, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467.
authors.forename: Jianmin
authors.initials: J
authors.lastname: Gao
keywords: cLac; cyclic peptide; lactadherin; native chemical ligation; phosphatidylserine