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Characterization of a set of HIV-1 protease inhibitors using binding kinetics data from a biosensor-based screen
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
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2000 (English)In: Journal of Biomolecular Screening, ISSN 1087-0571, E-ISSN 1552-454X, Vol. 5, no 5, 353-359 p.Article in journal (Refereed) Published
Abstract [en]

The interaction between 290 structurally diverse human immunodeficiency virus type 1 (HIV-1) protease inhibitors and the immobilized enzyme was analyzed with an optical biosensor, Although only a single concentration of inhibitor was used, information about the kinetics of the interaction could be obtained by extracting binding signals at discrete time points. The statistical correlation between the biosensor binding data, inhibition of enzyme activity (K-i), and viral replication (EC50) revealed that the association and dissociation rates for the interaction could be resolved and that they were characteristic for the compounds. The most potent inhibitors, with respect to K-i and EC50 values, including the clinically used drugs, all exhibited fast association and slow dissociation rates. Selective or partially selective binders for HIV-1 protease could be distinguished from compounds that showed a general protein-binding tendency by using three reference target proteins. This biosensor-based direct binding assay revealed a capacity to efficiently provide high-resolution information on the interaction kinetics and specificity of the interaction of a set of compounds with several targets simultaneously.

Place, publisher, year, edition, pages
2000. Vol. 5, no 5, 353-359 p.
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Natural Sciences Pharmaceutical Sciences
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URN: urn:nbn:se:uu:diva-51298DOI: 10.1177/108705710000500507ISI: 000165255900007PubMedID: 11080694OAI: oai:DiVA.org:uu-51298DiVA: diva2:79207
Available from: 2006-03-04 Created: 2006-03-04 Last updated: 2017-12-04Bibliographically approved

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Schaal, WesleyKarlén, AndersHallberg, AndersDanielson, U. Helena

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