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Research Article Open access CC BY 4.0

Biophysical Study for the Interactions of Some Diazo Dyes with Human Serum Albumin

Mohammed Hadi Al–Douh, Elham Abdalrahem Bin Selim, Edrees Muhammad Tahir, Sabah Ahmed Abdo Esmail, Yaman Ahmed Naji, Hassan Hadi Abdullah

Asian Journal of Applied Chemistry Research · pp. 1–10 · Published 28 Dec 2019

10.9734/ajacr/2019/v4i330113

Abstract

The biophysical interactions between the human serum albumin HSA and three synthesized diazo dyes 1-3 have been investigated by thermodynamic parameters and molecular docking technique. The binding constants Kb were calculated and the compounds were ranked according to their docking free energy. Different interactions were elucidated at the active site of the protein. Among these interactions is the hydrogen bonding which plays an essential role in the interaction with the protein. Both the theoretical and practical studies have agreed that diazo dye 1 has the strongest interaction with the active site.

Molecular docking diazo dyes nitro functional group human serum albumin HSA thermodynamic parameters hydrogen bonding.

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