Title:2’-Deoxyribose Mediated Glycation Leads to Alterations in BSA Structure Via Generation of Carbonyl Species
Volume: 21
Issue: 9
Author(s): Zeeshan Rafi, Sultan Alouffi, Mohd Sajid Khan*Saheem Ahmad*
Affiliation:
- Department of Bioscience, Integral University, Lucknow, 226026, UP,India
- College of Applied Medical Sciences, University of Ha’il, Ha’il,Saudi Arabia
Keywords:
Diabetes, bovine serum albumin, glycation, nitroblue tetrazolium, schiff base, amadori products, advanced glycation
end products (AGEs).
Abstract: The non-enzymatic glycosylation is a very common phenomenon in the physiological
conditions which is mediated by distinct chemical entities containing reactive carbonyl species (RCS)
and participates in the modification of various macromolecules particularly proteins. To date, various
carbonyl species, i.e., glucose, fructose, D-ribose and methylglyoxal have been used frequently to
assess the in-vitro non-enzymatic glycosylation. Similarly, 2'-Deoxyribose is one of the most abundant
reducing sugar of the living organisms which forms the part of deoxyribonucleic acid and may react
with proteins leading to the production of glycation intermediates, advanced glycation end products
(AGEs) and highly reactive RCS. Thymidine phosphorylase derived degradation of thymidine
contributes to the formation of 2'-Deoxyribose, therefore, acting as a major source of cellular 2'-
Deoxyribose. Since albumin is a major serum protein which plays various roles including binding and
transporting endogenous and exogenous ligands, it is more prone to be modified through different
physiological modifiers; therefore, it may serve as a model protein for in-vitro experiments to study the
effect of 2’Deoxyribose mediated modifications in the protein. In this study, Bovine Serum Albumin
(BSA) was glycated with 50 and 100 mM 2'-Deoxyribose followed by examining secondary and
tertiary structural modifications in BSA as compared to its native (unmodified) form by using various
physicochemical techniques. We evident a significant modification in 2'-Deoxyribose-glycated BSA
which was confirmed through increased hyperchromicity, keto amine moieties, carbonyl and
hydroxymethylfurfural content, fluorescent AGEs, altered secondary structure conformers (α helix and
β sheets), band shift in the amide-I region and diminished free lysine and free arginine content. These
modifications were reported to be higher in 100 mM 2'-Deoxyribose-glycated BSA than 50 mM 2'-
Deoxyribose-glycated BSA. Our findings also demonstrated that the rate of glycation is positively
affected by the increased concentration of 2'-Deoxyribose. The results of the performed study can be
implied to uncover the phenomenon of serum protein damage caused by 2'-Deoxyribose leading
towards diabetic complications and the number of AGE-related diseases.
