Biophysical insight into the interaction mechanism of plant derived polyphenolic compound tannic acid with homologous mammalian serum albumins

International Journal of Biological Macromolecules
Mohd IshtikharRizwan Hasan Khan

Abstract

Numerous phenolic compounds have been reported in the last decade that have a good antioxidant property and interaction affinity towards mammalian serum albumins. In the present study, we have utilized mammalian serum albumins as a model protein to examine their comparative interaction property with polyphenolic compound tannic acid (TA) by using various spectroscopic and calorimetric methods We have also monitored the esterase and antioxidant activity of mammalian serum albumins in the absence and presence of TA. The obtain results recommended that the TA have a good binding affinity (∼104 to 106M-1) towards mammalian serum albumins and shows double sequential binding sites, which depends on the concentration of TA that induced the conformational alteration which responsible for the thermal stability of proteins. Binding affinity, structural transition and thermodynamic parameters were calculated from spectroscopic and calorimetric method reveals that non-covalent interaction causes partial conformational alteration in the secondary structure of protein ie.; increase in α-helical content with decrease in β-sheet, random coil and other structure. Meanwhile, we have found that esterase activities of serum albumins were also stab...Continue Reading

Citations

Jul 19, 2019·Journal of Biomolecular Structure & Dynamics·Ludmila AricovDan-Florin Anghel
Aug 4, 2020·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Monidipa Konar, Harekrushna Sahoo
Jan 15, 2020·ACS Chemical Neuroscience·Aiman MasroorRizwan Hasan Khan
Sep 6, 2021·International Journal of Biological Macromolecules·Mohd IshtikharRizwan Hassan Khan
Jan 8, 2022·Journal of Biomaterials Applications·Andrew Baldwin, Brian W Booth

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