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Updated: May 3, 2026

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
Published on: August 7, 2021
Computational inhibition studies of the human proteasome by argyrin-based analogues with subunit specificity
Eriketi Z Loizidou1, Constantinos D Zeinalipour-Yazdi
1Department of Biological Sciences, University of Cyprus, Nicosia, 1678, Cyprus.
Abstract:
A computational procedure was developed to study the subunit-specific interactions of the proteasome inhibitors argyrin A and F, with the aim of indentifying the determinants of subunit selectivity. Three-dimensional models of humanized proteasome active sites β1 , β2 and β5 were developed and subsequently used in molecular docking simulations with the argyrin analogues. The subunit selectivity exhibited by each analogue could be explained based on the site-specific interactions and a probability-based specificity parameter derived in this study. A rational approach that involved maximizing site-specific interactions was followed to guide the design of new argyrin analogues as specific inhibitors of the caspase-like (β1 site) activity.
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