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

Main Article Content

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

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.

Article Details

How to Cite
Hadi Al–Douh, M., Abdalrahem Bin Selim, E., Muhammad Tahir, E., Ahmed Abdo Esmail, S., Ahmed Naji, Y., & Hadi Abdullah, H. (2019). Biophysical Study for the Interactions of Some Diazo Dyes with Human Serum Albumin. Asian Journal of Applied Chemistry Research, 4(3), 1-10. https://doi.org/10.9734/ajacr/2019/v4i330113
Section
Original Research Article

References

Morris GM, Lim-Wilby M. Molecular docking, chapter 19. In: Kukol A, editor. Methods in Molecular Biology, Molecular Modeling of Proteins, Humana Press, Totowa, New Jersey, USA. 2008;443:365-382.
DOI: 10.1007/978-1-59745-177-2
[ISBN: 978-1-58829-864-5]

Lanez T, Lanez E. A molecular docking study of N-ferrocenylmethylnitroanilines as potential anticancer drugs. Intern J Pharmaco Phytochem Ethnomed. 2016; 2:5-12. DOI:10.18052/www.scipress.com/IJPPE.2.5

Li S, Wawrzyniak J, Queneau Y, Soulere L. 2-Substituted aniline as a simple Scaffold for LuxR-regulated QS modulation. Molecules. 2017;22(2090):1-10.
DOI: 10.3390/molecules22122090

Gu Y, Wang Y, Zhang H. Study on the interactions between toxic nitro aniline and lysozyme by spectroscopic approaches and molecular modelling, spectrochim acta Part A: Mol Biomol Spectro. 2018;202:260-268.
DOI: 10.1016/j.saa.2018.05.008

Tabassum S, Yadav S, Ahmad I. Heterobimetallic o-vanillin functionalized complexes: In vitro DNA binding validation, cleavage activity and molecular docking studies of CuII–Sn2IV analogs. J Organomet Chem. 2014;752:17-24.
DOI: 10.1016/j.jorganchem.2013.11.023

Khan P, Rahman S, Queen A, Manzoor S, Naz F, Hasan GM, Luqman S, Kim J, Islam A, Ahmad F, Hassan MI. Elucidation of dietary polyphenolics as potential inhibitor of microtubule affinity regulating Kinase 4: In silico and In vitro studies. Scientific Rep. 2017;7:9470.
DOI: 10.1038/s41598-017-09941-4

Siddiqui GA, Siddiqi MK, Khan RH, Naeem A. Probing the binding of phenolic aldehyde vanillin with bovine serum albumin: Evidence from spectroscopic and docking approach. Spectrochim Acta Part A: Mol Biomol Spectro. 2018;203:40- 47.
DOI: 10.1016/j.saa.2018.05.023

Zarei L, Asadi Z, Dusek M, Eigner V. Homodinuclear Ni (II) and Cu (II) Schiff base complexes derived from o-vanillin with a pyrazole bridge: Preparation, crystal structures, DNA and protein (BSA) binding, DNA cleavage, molecular docking and cytotoxicity study. J Photochem Photobio A: Chem. 2019;374:145-160.
DOI: 10.1016/j.jphotochem.2019.02.001

Kavitha B, Sravanthi M, Reddy PS. DNA interaction, docking, molecular modelling and biological studies of o-vanillin derived Schiff base metal complexes J Molec Struc. 2019;1185:153-167.
DOI: 10.1016/j.molstruc.2019.02.093

De A, Ray HP, Jain P, Kaur H, Singh N. Synthesis, characterization, molecular docking and DNA cleavage study of transition metal complexes of o-vanillin and glycine derived Schiff base ligand. J Molec Struc. 2020;1199:126901.
DOI: 10.1016/j.molstruc.2019.126901

Dehghanian F, Kay M, Kahrizi D. A novel recombinant AzrC protein proposed by molecular docking and in silico analyses to improve azo dye's binding affinity. Gene. 2015;569:233-238.
DOI: 10.1016/j.gene.2015.05.063

El-Sonbati AZ, Mohamed GG, El-Bindary AA, Hassan WMI, Diab MA, Morgan SM, Elkholy AK. Supramolecular structure, molecular docking and thermal properties of azo dye complexes. J Molec Liq. 2015; 212:487-502.
DOI: 10.1016/j.molliq.2015.09.038

El-Bindary AA, Mohamed GG, El-Sonbati AZ, Diab MA, Hassan WMI, Morgan SM, Elkholy AK. Geometrical structure, potentiometric, molecular docking and thermodynamic studies of azo dye ligand and its metal complexes. J Molec Liq. 2016;218:138-149.
DOI: 10.1016/j.molliq.2016.02.021

Srinivasan S, Sadasivam SK. Exploring docking and aerobic-microaerophilic biodegradation of textile azo dye by bacterial systems. J Water Process Eng. 2018;22:180-191.
DOI: 10.1016/j.jwpe.2018.02.004

Franco JH, da Silva BF, Dias EFG, de Castro AA, Ramalho TC, Zanoni MVB. Influence of auxochrome group in disperse dyes bearing azo groups as chromophore center in the biotransformation and molecular docking prediction by reductase enzyme: Implications and assessment for environmental toxicity of xenobiotics. Ecotoxi Enviro Safety. 2018;160:114-126. DOI: 10.1016/j.ecoenv.2018.04.066

Zubair MS, Alarif WM, Ghandourah MA, Anam S. A new steroid glycoside from Begonia sp.: Cytotoxic activity and docking studies. Nat Prod Res; 2019. (in press).
DOI: 10.1080/14786419.2019.1669026

Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K. Crystal structure of human serum albumin at 2.5 Å resolution. Protein Eng. 1999;12:439–446.
DOI: 10.1093/protein/12.6.439

Zunszain PA, Ghuman J, Komatsu T, Tsuchia E, Curry S. Crystal structural analysis of human serum albumin complexed with hemin and fatty acid. BMC Structural Biology. 2003;3(6):1-9.
Available:http://www.biomedcentral.com/1472-6807/3/6

Levitt DG, Levitt MD. Human serum albumin homeostasis: A new look at the roles of synthesis, catabolism, renal and gastrointestinal excretion, the clinical value of serum albumin measurements. Intern J General Med. 2016;9:229-255.
DOI: 10.2147/IJGM.S102819

Taverna M, Marie AL, Mira JP, Guidet B. Specific antioxidant properties of human serum albumin. Ann Intensive Care. 2013; 3(4):1-7.
DOI: 10.1186/2110-5820-3-4

Shaif LM, Al-Hazmi AA, Esmail SAA, Al-Asbahy WM, Al-Fkeeh RA. Synthesis, characterization and interaction studies of carbohydrizide derivatives based drug with human serum albumin (HSA): Spectroscopic and molecular docking investigations. AASCIT Intern J Chem Biomed Sci. 2016;2(3):17-27.
[ISSN: 2472-9590]

Al-Hazmi AA, Al-Asbahy WM, Aqlan F, Esmail SAA, Shamsi M, Al-Sabahi SM, Shaif LM. Synthesis and characterization of some carbohydrizide derivatives: Interaction studies with human serum albumin (HSA), molecular docking and photo–induced cleavage. AASCIT J Chem. 2019;5(1):1-13. Available:http://www.aascit.org/journal/chemistry

Esmail SAA, Shamsi M, Al-Asbahy WM. Interaction and photo–induced cleavage studies of meropenem drug with human serum albumin using spectroscopic and molecular docking investigations. J Biomolec Struc Dynam. 2018;37:3282-3289.
DOI: 10.1080/07391102.2018.1509731

Esmail SAA, Shamsi M, Chen T, Al-Asbahy WM. Design, synthesis and characterization of tin‐based cancer chemotherapy drug entity: In vitro DNA binding, cleavage, induction of cancer cell apoptosis by triggering DNA damage‐mediated p53 phosphorylation and molecular docking. Appl. Organometal. Chem. 2018;e4651:1-14.
DOI: 10.1002/aoc.4651

Al–Douh MH, Selim EAB, Al–Haik WM, Mahram SMB, Al–Bakri AK, Al–Nohey DS, Sonbol KS. Synthesis and antimicrobial activity of some compounds derived from diazo dyes. Intern J Chem Stud. 2019;3(4): 06-12.
[ISSN: 2581-348X]

Selim EAB, Al–Douh MH. Unusual effects of intramolecular hydrogen bonds and dipole interaction on FTIR and NMR of some imines. Asian J Appl Chem Res. 2019;3(3):1-6.
DOI: 10.9734/AJACR/2019/v3i330096

Al–Douh MH, Salim HAM, Selim EAB, Abdullah HH. Molecular structure and spectroscopic studies of some diazo dyes compounds using DFT method. Toward Intelligent solutions for developing and empowering our societies. The first International Conference of Intelligent Computing and Engineering ICOICE-2019, Mukalla, Hadhramout, Yemen. Computing and Engineering. IEEE. (In press). 2019; 49. 978-1-7281-4487-0/19/$31.00 ©2019 IEEE

Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 1995;4:2411-2423.
DOI: 10.1002/pro.5560041120

Tabassum S, Al-Asbahy WM, Afzal M, Arjmand F. Synthesis, characterization and interaction studies of copper based drug with human serum albumin (HSA): Spectroscopic and molecular docking investigations. J Photochem Photobio B: Biology. 2012;114:132-139.
DOI: 10.1016/j.jphotobiol.2012.05.021

Pedretti A, Villa L, Vistoli G. VEGA – An open platform to develop chemo-bio-informatics applications, using plug-in architecture and script programming. J Computer-Aided Molec Design. 2004;18: 167-173.
DOI:10.1023/b:jcam.0000035186.90683.f2

Cheung J, Rudolph MJ, Burshteyn F, Cassidy MS, Gary EN, Love J, Franklin MC, Height JJ. Structures of human acetylcholinesterase in complex with pharmacologically important ligands. J Med Chem. 2012;55(22):10282-10286.
DOI: 10.1021/jm300871x

Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS, Olson AJ Autodock4 and AutoDockTools4: Automated docking with selective receptor flexiblity J Comput Chem. 2009;16:2785-2791.
DOI: 10.1002/jcc.21256

Zhang YZ, Zhou B, Liu YX, Zhou CX, Ding XL, Liu Y. Fluorescence study on the interaction of bovine serum albumin with p-aminoazobenzene. J Fluoresc. 2008;18: 109-118.
DOI: 10.1007/s10895-007-0247-4

Ross PD, Subramanian S. Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry. 1981;20(11):3096-3102.
DOI: 10.1021/bi00514a017