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- W2384994026 abstract "Aim ADS-J1 is a low molecular HIV entry inhibitor targeting HIV transmembrane subunit gp41 through virtual screening from a compound library containing 20 000 molecules. This study is to investigate the binding sites of ADS-J1 on gp41. Methods Acid native polyacrylamide gel electrophoresis (AN-PAGE) assay was applied to test the binding ability of ADS-J1 with the peptides derived from gp41 N-terminal heptad repeat (NHR) region. Results It was reported previously that ADS-J1 could block the gp41 six-helix bundle (6-HB) formation using native polyacrylamide gel electrophoresis (N-PAGE). However,the binding sites could not be found because positive charged N-peptides derived from gp41 NHR could not show bands on the gel. In the present study,the AN-PAGE assay which could show N-peptides in the gel was established,and it was found that ADS-J1 could inhibit the gp41 6-HB formation. Moreover,ADS-J1 bound directly to the gp41 cavity region of NHR. The positively charged residue (K574) located in this region was critical for the binding of ADS-J1. Conclusions ADS-J1 inhibits HIV entry by targeting the cavity region of gp41 NHR,whereas K574 in the cavity plays a critical role for the binding. Furthermore,the AN-PAGE assay provides a simple method for studying the mechanism of action of virus entry inhibitors targeting the transmembrane protein of type I enveloped virus." @default.
- W2384994026 created "2016-06-24" @default.
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- W2384994026 date "2010-01-01" @default.
- W2384994026 modified "2023-09-23" @default.
- W2384994026 title "Acid native polyacrylamide gel electrophoresis:a method for studying the mechanism of action of HIV entry inhibitor ADS-J1" @default.
- W2384994026 hasPublicationYear "2010" @default.
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