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

Published

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