Thermodynamic profiling of conformationally constrained cyclic ligands for the PDZ domain.
Journal Article
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.
Full Text
Duke Authors
Cited Authors
- Li, T; Saro, D; Spaller, MR
Published Date
- March 2004
Published In
Volume / Issue
- 14 / 6
Start / End Page
- 1385 - 1388
PubMed ID
- 15006367
Pubmed Central ID
- 15006367
Electronic International Standard Serial Number (EISSN)
- 1464-3405
International Standard Serial Number (ISSN)
- 0960-894X
Digital Object Identifier (DOI)
- 10.1016/j.bmcl.2003.09.103
Language
- eng