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Comprehending renin inhibitor's binding affinity using structure-based approaches

Comprehending renin inhibitor's binding affinity using structure-based approaches

Bioorganic and Medicinal Chemistry Letters 23(24): 6667-6672

The performance of several structure-based design (SBD) approaches in predicting the binding affinity of diverse small molecule inhibitors co-crystallized to human renin was assessed to ascertain the modeling tool and method of choice required when dealing with structure-based lead optimization projects. Most of the SBD approaches investigated here were able to provide qualitative guidance, but quantitative accuracy as well as decisive discrimination between [in]actives is still not within reach. Such an outcome suggests that the current methods need improvement to capture the overall physics of the binding phenomenon for consistent applications in a lead optimization setting.

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Accession: 052269481

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PMID: 24239018

DOI: 10.1016/j.bmcl.2013.10.044

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