1. Mechanism of anti-HIV activity of negatively charged albumins: biomolecular interaction with the HIV-1 envelope protein gp120
- Author
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Kuipers, M.E., Huisman, J.G., Swart, P.J., De Bethune, M.-P., Pauwels, R., Schuitemaker, H., De Clercq, E., and Meijer, D.K.F.
- Subjects
Albumin -- Research ,Anions -- Research ,Viral envelopes -- Research ,HIV (Viruses) -- Research ,Health - Abstract
Negatively charged proteins called albumins seem capable of binding to parts of the gp120 envelope protein of HIV. The gp120 protein is involved in binding the virus to the CD4 receptor on the surface of T cells. Researchers used a chemical process to attach negatively-charged carboxyl groups to human serum albumin to create negatively charged albumins (NCAs). The NCAs were tested against several artificially synthesized amino acid sequences representing various parts of the gp120 protein. The NCAs bound only to the V3 region and the C-terminus of gp120. The NCA with the most lysine groups modified had the greatest affinity for the V3 region. This NCA also was most active against HIV in viral assays. Monoclonal antibodies against the V3 region blocked the binding of NCAs to the synthetic peptide. The binding appears to be electrostatic in nature, since the V3 region is positively charged.
- Published
- 1996