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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.

Cited by 4

Electronic Structure of Two New Bis-Schiff Base Ligands using DFT Method

Elham Abdalrahem Bin Selim, Mohammed Hadi Al–Douh, H. H. Abdullah · Asian Journal of Applied Chemistry Research · 2021

Molecular Structure and Spectroscopic Studies of Some Diazo Dyes Compounds using DFT Method

Mohammed Hadi Al–Douh, Elham Abdalrahem Bin Selim, Haydar A. Mohammad Salim · 2019 First International Conference of Intelligent Computing and Engineering (ICOICE) · 2019

Synthesis, Characterization and Biological Activity of New Amides Containing Azo Moieties

Elham Abdalrahem Bin Selim, Mohammed Hadi Al-Douh, Samia Mabrook Bin Mahram · 2022

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