<p>Complexation between new hetarylazo dyes containing dihydroquinoline and tetrazole moieties and human serum albumin (HSA) was studied. According to the spectrophotometry results, the dyes predominantly exist in the protein matrix in the anionic and neutral forms depending on the dye structure and pH. The binding constants at various pH were determined by the method of HSA fluorescence quenching by the dye. They depend on the dye form and are equal to 8.2•10<sup>4</sup> and (1.3–2.2)•10<sup>4</sup> L mol<sup>−1</sup> for the anionic and neutral form, respectively. Possible sites of preferential binding of the dyes under study were determined by molecular docking.</p>

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Complexation of serum albumin with new hetarylazo dyes with dihydroquinoline and tetrazole moieties

  • G. V. Golovina,
  • E. N. Khodot,
  • E. V. Radchenko,
  • V. A. Palyulin,
  • V. A. Kuzmin,
  • T. D. Nekipelova

摘要

Complexation between new hetarylazo dyes containing dihydroquinoline and tetrazole moieties and human serum albumin (HSA) was studied. According to the spectrophotometry results, the dyes predominantly exist in the protein matrix in the anionic and neutral forms depending on the dye structure and pH. The binding constants at various pH were determined by the method of HSA fluorescence quenching by the dye. They depend on the dye form and are equal to 8.2•104 and (1.3–2.2)•104 L mol−1 for the anionic and neutral form, respectively. Possible sites of preferential binding of the dyes under study were determined by molecular docking.