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Updated: Aug 25, 2026

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
Published on: June 23, 2026
Thermodynamic profiling of conformationally constrained cyclic ligands for the PDZ domain
Tao Li1, Dorina Saro, Mark R Spaller
1Department of Chemistry, Wayne State University, Detroit, MI 48202, USA.
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.
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