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

Spaller, Mark Robert

Cited Authors

Li, T; Saro, D; Spaller, MR

Published Date

March 2004

Published In

Bioorganic & Medicinal Chemistry Letters

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

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