Correlation of Experimental and Calculated Inhibition Constants of Protease Inhibitor Complexes.

ABSTRACT: Predicting the potency of inhibitors is key to in silico screening of promising synthetic or natural compounds. Here we describe a predictive workflow that provides calculated inhibitory values, which concord well with empirical data. Calculations of the free interaction energy ΔG with the YASARA plugin FoldX were used to derive inhibition constants K_i from PDB coordinates of protease-inhibitor complexes. At the same time, corresponding K_D values were obtained from the PRODIGY server. These results correlated well with the experimental values, particularly for serine proteases. In addition, analyses were performed for inhibitory complexes of cysteine and aspartic proteases, as well as of metalloproteases, whereby the PRODIGY data appeared to be more consistent. Based

SUBMITTER: Goettig P 

PROVIDER: S-EPMC10889394 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature