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Fungal-Selective Resorcylate Aminopyrazole Hsp90 Inhibitors: Optimization of Whole-Cell Anticryptococcal Activity and Insights into the Structural Origins of Cryptococcal Selectivity

Paul T. Marcyk, Emmanuelle V. LeBlanc, D.A. Kuntz, Alice Xue, Francisco Ortiz, Richard Trilles, Stephen Bengtson, Tristan M. G. Kenney, David S. Huang, Nicole Robbins, Noelle S. Williams, Damian J. Krysan, Gilbert G. Privé, Luke Whitesell, Leah E. Cowen, Lauren E. Brown

2021Journal of Medicinal Chemistry39 citationsDOIOpen Access PDF

Abstract

Hsp90 nucleotide binding domain (NBD), as the apoprotein and in complexes with the non-species-selective Hsp90 inhibitor NVP-AUY922 and three RAPs revealing unique ligand-induced conformational rearrangements, which reaffirm the hypothesis that intrinsic differences in protein flexibility can confer selective inhibition of fungal versus human Hsp90 isoforms.

Topics & Concepts

Cryptococcus neoformansHsp90Candida albicansGene isoformChemistryHsp90 inhibitorBiochemistryMicrobiologyBiologyHeat shock proteinGeneToxin Mechanisms and ImmunotoxinsMicrobial Natural Products and BiosynthesisFungal Infections and Studies
Fungal-Selective Resorcylate Aminopyrazole Hsp90 Inhibitors: Optimization of Whole-Cell Anticryptococcal Activity and Insights into the Structural Origins of Cryptococcal Selectivity | Litcius