Abstract
A new method is found for the detection of interactions between a highly anti-HIV (human immunodeficiency virus) active curdlan sulfate (CS) and a HIV peptide with the aid of NMR spectroscopy. To elucidate the action mechanism of the anti-HIV activity in curdlan sulfate, a partial peptide sequence in an envelope glycoprotein gp120 was synthesized. The sequence consists of a dimer (D518) of the sequence from no. 506 to 518, which is one of putative reaction sites for the sulfated polysaccharide. This was used to examine its interactions with CS. When CS and D518 were mixed in appropriate molar ratios, gel-like materials were formed. 1H NMR spectra of the gel-like material revealed the formation of interpolymeric ionic interactions between a negatively charged CS and a positively charged D518. At the molar ratio [CS]/[D518] of 0.27, 100% gel formation was observed. Effects of molar ratio, pH, and temperature on the gel formation, that is, the degree of interaction, were also studied. In addition, although f...
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