Docking and structure activity relationship studies of potent and selective thiazolidinethione GSK-3 inhibitors
Year: 2024
Type: article
Abstract: Glycogen synthase kinase-3 (GSK-3) plays a key role in several biochemical pathways and is an attractive target for pharmacological intervention. We prepared a series of analogs of a highly selective thiazolidinethione inhibitor of GSK-3. The structure-activity relationship indicated a precise structural requirement for potent inhibition. We used docking and bioinformatic analysis to explore the rationale for the potency and selectivity of this class of GSK-3 inhibitors. These computational studies identified residues unique to GSK-3 likely to play a role in ligand-specific induced fit interactions. Together, these studies highlight the structural stringency of specific kinase inhibition that can be achieved for GSK-3.
Authors: Hannah Boesger, Kurtis Williams, Sa Adatu Abdullai, Brianna Hubble, Mahboubeh S. Noori, Crina Orac, Deborah K. Amesaki, Davoud Ghazanfari, Emily A. Fairchild, Opeyemi O. Fatunbi, Joshua A. Pritchard, Douglas J. Goetz, Jennifer V. Hines, Stephen C. Bergmeier
Institution: Ohio University
Language: English
Subfield: Computational Theory and Mathematics
Field: Computer Science
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,770
OpenAlex ID: W4405430992