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Understanding lipid recognition by protein-mimicking cyclic peptides

Authors
Journal
Tetrahedron
0040-4020
Publisher
Elsevier
Publication Date
Volume
70
Issue
42
Identifiers
DOI: 10.1016/j.tet.2014.07.104
Keywords
  • Cyclic Peptide
  • Native Chemical Ligation
  • Phosphatidylserine
  • Lactadherin
  • Clac
Disciplines
  • Biology
  • Chemistry
  • Design

Abstract

Abstract This paper describes our investigation of the structural determinants of a designed cyclic peptide (cLac, cyclic peptide mimicking lactadherin) (Zheng, H.; Wang, F.; Wang, Q.; Gao, J. J. Am. Chem. Soc.2011, 133, 15280–15283) for 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.

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