کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5216527 | 1383267 | 2014 | 7 صفحه PDF | دانلود رایگان |
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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Journal: Tetrahedron - Volume 70, Issue 42, 21 October 2014, Pages 7632–7638