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Article

Structural basis for the resilience of Darunavir (TMC114) resistance major flap mutations of HIV-1 protease.

Interdisciplinary sciences, computational life sciences - 1 Dec 2009

Purohit Rituraj, Sethumadhavan Rao

Abstract excerpt

To understand the origin of the apparent low sensitivity to mutations exhibited by Darunavir, the binding energetics of this inhibitor to the HIV-1 protease was studied. Our research indicates that the observed effectiveness of Darunavir against the wild type HIV-1 protease is due to an extremely high affinity towards the wild-type and a relatively mild effect to the I50V and I54M mutations is due to low affinity...

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Source

Identifiers

PMID: 20640812
DOI: 10.1007/s12539-009-0043-8

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Structural basis for the resilience of Darunavir (TMC114) resistance major flap mutations of HIV-1 protease.PMID 20640812Read ↗

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