Biophysical Study for the Interactions of Some Diazo Dyes with Human Serum Albumin
Mohammed Hadi Al–Douh *
Department of Chemistry, Faculty of Science, Hadhramout University, Mukalla, Hadhramout, Yemen.
Elham Abdalrahem Bin Selim
Department of Chemistry, Faculty of Science, Hadhramout University, Mukalla, Hadhramout, Yemen.
Edrees Muhammad Tahir
Department of Physics, College of Education, Salahaddin University–Erbil, Erbil, Iraq.
Sabah Ahmed Abdo Esmail
Department of Chemistry, Faculty of Science, Ibb University, Ibb, Yemen.
Yaman Ahmed Naji
Department of Biochemistry, Faculty of Science, Ibb University, Ibb, Yemen.
Hassan Hadi Abdullah
Department of Chemistry, College of Education, Salahaddin University–Erbil, Erbil, Iraq.
*Author to whom correspondence should be addressed.
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.
Keywords: Molecular docking, diazo dyes, nitro functional group, human serum albumin HSA, thermodynamic parameters, hydrogen bonding.