期刊
JOURNAL OF CHEMICAL INFORMATION AND MODELING
卷 60, 期 2, 页码 880-889出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jcim.9b00847
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资金
- Fundacao de Amparo a Pesquisa do Estado de sao Paulo FAPESP [2013/18009-4, 2018/21749-3]
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Coordenacio de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
One tactic for cysteine protease inhibition is to form a covalent bond between an electrophilic atom of the inhibitor and the thiol of the catalytic cysteine. In this study, we evaluate the reaction free energy obtained from a hybrid quantum mechanical/molecular mechanical (QM/MM) free energy profile as a predictor of affinity for reversible, covalent inhibitors of rhodesain. We demonstrate that the reaction free energy calculated with the PM6/MM potential is in agreement with the experimental data and suggest that the free energy profile for covalent bond formation in a protein environment may be a useful tool for the inhibitor design.
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