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Title 

High-throughput screening method of inhibitors that block the interaction between 2 helical regions of HIV-1 gp41

Authors 

B S JinW K LeeK AhnMyung Kyu LeeY G Yu

Publisher 

SAGE Publications (UK and US)

Issue Date 

2005

Citation 

Journal of Biomolecular Screening, vol. 10, no. 1, pp. 13-19

Keywords 

gp41HIV-1inhibitormembrane fusionscreeningglycoprotein gp 41human immunodeficiency virus fusion inhibitorky 001ky 002protein inhibitor

Abstract 

The HIV-1 envelope glycoprotein transmembrane subunit, gp41, mediates the fusion of viral and target cell membranes. The 2 helical regions in the ectodomain of gp41, the N-helix and the C-helix, form a helical bundle complex that has been suggested as a fusion-active conformation. Previously, an enzyme-linked immunosorbent assay (ELISA) method had been established to measure the interaction of 2 helical regions of gp41. In this study, the ELISA method was modified to apply high-throughput screening (HTS) of an organic compound library. A few compounds had been identified to prevent the interaction between 2 helical regions of gp41, and they were further shown to inhibit the gp41-mediated viral infection. In addition, they specifically quenched the fluorescence of tryptophan in the N-helix region, indicating that these compounds bound to the N-helix rather than the C-helix of gp41. These results suggested that this assay method targeting gp41 could be used for HTS of HIV fusion inhibitors.

ISSN 

1087-0571

Link 

http://dx.doi.org/10.1177/1087057104269726

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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