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• W2004357713 abstract "The key role of gp120 in the cellular entry of HIV makes this glycoprotein an attractive target for new drugs. Various polyanions bind to the positively charged V3 loop of gp120. Here, we consider a series of anionic porphyrins bearing two sulfonate groups and two carboxylic chains with various degree of esterification. These molecules carry an overall negative charge between 4 and 2. Upon activation by light, these compounds, known as photosensitizers, produce highly reactive oxygen species able to damage amino acid chains. The interactions of these molecules with the V3 loop and a positively charged area in the C5 region were investigated in the dark by using specific antibodies and ELISA protocols. Competitive inhibition of the anti-V3 antibody was observed with an increased efficiency for the esterified compounds. No evidence for binding to the C5 region was found. In contrast, when gp120 was irradiated with light in presence of the porphyrin prior to the addition of the antibody, strong inhibition of the anti-C5 antibody was observed revealing irreversible photo-damages in this region. No effect on the V3 loop was observed. Irradiations at two wavelengths made it possible to identify porphyrin monomers as the photoactive forms despite the presence of large excess of dimers in the incubation solution. It is suggested that porphyrins bound to the V3 loop could produce photo-damages at some distance, in particular within the C5 region that contains several photosensitive amino acids." @default.
• W2004357713 created "2016-06-24" @default.
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• W2004357713 date "2004-01-01" @default.
• W2004357713 modified "2023-09-25" @default.
• W2004357713 title "Interaction of sulfonated anionic porphyrins with HIV glycoprotein gp120: photodamages revealed by inhibition of antibody binding to V3 and C5 domains" @default.
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• W2004357713 doi "https://doi.org/10.1016/s0166-3542(03)00176-1" @default.
• W2004357713 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14670592" @default.
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