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Thermodynamic profiling of conformationally constrained cyclic ligands for the PDZ domain.

作者信息

Li Tao, Saro Dorina, Spaller Mark R

机构信息

Department of Chemistry, Wayne State University, Detroit, MI 48202, USA.

出版信息

Bioorg Med Chem Lett. 2004 Mar 22;14(6):1385-8. doi: 10.1016/j.bmcl.2003.09.103.

DOI:10.1016/j.bmcl.2003.09.103
PMID:15006367
Abstract

Inspired by structure-based design and tailored for combinatorial preparation, a series of novel cyclic peptides has been developed to yield binding ligands for the third PDZ domain (PDZ3) of PSD-95. These side chain-side chain bridged peptides permit the systematic expansion or contraction of ring size, which is intended to maximize the conformational diversity of the ensemble. Isothermal titration calorimetry (ITC) was used to measure the dissociation constants (K(d)) and associated thermodynamic binding parameters.

摘要

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