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Analysis of interaction between sulfated polysaccharides and HIV oligopeptides by surface plasmon resonance

Battulga, Tungalag, Tumurbaatar, Oyunjargal, Ganzorig, Oyundelger, Ishimura, Takahisa, Kanamoto, Taisei, Nakashima, Hideki, Miyazaki, Kensuke, Yoshida, Takashi
International journal of biological macromolecules 2019 v.125 pp. 909-914
Human immunodeficiency virus, antiretroviral agents, antiretroviral properties, arginine, curdlan, dextran, dissociation, electrostatic interactions, glycoproteins, light scattering, lysine, models, molecular weight, oligopeptides, particle size, sulfates, surface plasmon resonance, zeta potential
This study aims to quantitatively investigate the interaction between sulfated polysaccharides with potent anti-HIV activity, dextran and curdlan sulfates with negatively charged sulfate groups, and poly-L-lysine as a model protein and oligopeptides from a HIV surface glycoprotein gp120 with positively charged amino acids using surface plasmon resonance (SPR) and dynamic light scattering (DLS) to elucidate the anti-HIV mechanism of sulfated polysaccharides. The apparent association- (ka) and dissociation rate (kd) constants of dextran and curdlan sulfates against poly-L-lysine were ka = 6.92 × 104–2.17 × 106 1/Ms and kd = 4.29 × 10−5–2.22 × 10−4 1/s; these kinetic constants were dependent on the molecular weights and degree of sulfation of sulfated polysaccharides. For interaction, the three oligopeptides from the HIV gp120 were peptide A 297TRPNNNTRKRIRIQRGPGRA316 with several lysine (K) and arginine (R) in the V3 loop region, peptide B 493PLGVAPTKAKRRVVQREKR511 with several K and R in the C-terminus region, and oligopeptide C 362KQSSGGDPEIVTHSFNCGG380 with few basic amino acids in the CD4 binding domain. Sulfated polysaccharides exhibited strong interaction against oligopeptides A and B, (ka = 5.48 × 104–2.96 × 106 1/Ms. and kd = 1.74 × 10−4–6.24 × 10−3 1/s), no interaction was noted against oligopeptide C. Moreover, the particle size and zeta potential by DLS indicated the interaction between sulfated polysaccharides and oligopeptides A and B, suggesting the anti-HIV mechanism of sulfated polysaccharides to be the electrostatic interaction of negatively charged sulfated polysaccharides and HIV at the positively charged amino acid regions.