New insights into non-enzymatic glycation of human serum albumin biopolymer: A study to unveil its impaired structure and function

Raghav, A. and Ahmad, J. and Alam, K. and Khan, A.U. (2017) New insights into non-enzymatic glycation of human serum albumin biopolymer: A study to unveil its impaired structure and function. International Journal of Biological Macromolecules, 101. pp. 84-99. ISSN 1418130

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Abstract

Albumin glycation and subsequent formation of advanced glycation end products (AGEs) correlate with diabetes and associated complications. Human Serum Albumin (HSA) was modified with D-glucose for a 40 day period under sterile conditions at 37 °C. Modified samples along with native HSA (unmodified) were analyzed for impairment in biochemical characteristics ((fructosamine, carbonyl, thiol, lysine, arginine, hydroxymethyl furfural [HMF] content), electrochemical (electrical conductance), simulated gastric fluid assay, simulated intestinal fluid assay, spectroscopic properties (UV, fluorescence), optical (surface contact angle) and fluid dynamics (viscosity and Stokes radius). Impairment in drug binding capacity of glycosylated-HSA was assessed with molecular docking experiment using metformin. UV-absorbance and fluorescence measurement were performed for drug bound glycated and native–HSA. Extensively modified HSA has been used to study its relevance in diabetes mellitus. Glucose modified-HSA resulted in AGEs formation. It suggests deleterious impairment in biochemical, electrochemical, spectroscopic, optical and fluidity properties of HSA at high concentrations of glucose. The results of the present study can be useful to understand the phenomenon of proteins damage in hyperglycemic conditions.

Item Type: Article
Uncontrolled Keywords: Advanced glycation end products; Albumin; Diabetes mellitus; Glucose; Glycation; Proteomics
Subjects: R Medicine > R Medicine (General)
Divisions: Faculties > Faculty of Life Sciences > Department of Biochemistry
Depositing User: AMU Library
Date Deposited: 23 Jan 2018 04:29
Last Modified: 23 Jan 2018 04:29
URI: http://ir.amu.ac.in/id/eprint/10907

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