Glycation of Immunoglobulin-G from Pentose Sugar: A Cause for Structural Perturbations

Title:Glycation of Immunoglobulin-G from Pentose Sugar: A Cause for Structural Perturbations

Volume: 23 Issue: 11

Author(s): Fahaad Alenazi*, Mohd Saleem, Azharuddin Sajid Syed Khaja, Mubashir Zafar, Mohammed Salem Alharbi, Turki Al Hagbani, Mohd Yasir Khan and Saheem Ahmad*

Affiliation:

• Department of Pharmacology, College of Medicine, University of Hail, Hail-2440, Saudi Arabia

• Department of Medical Laboratory Science, University of Hail, Hail-2440, Saudi Arabia

Keywords: Advanced glycation end-products, amadori product, 2’-deoxyribose, immunoglobulin-G, NBT assay, FT-IR.

Abstract:

Background: Glycation of immunoglobulin-G (IgG) molecules with monosaccharides may cause significant structural disability, thus resulting in their loss of function. The accumulation of AGEs formed from glycation plays an important role in the aliments associated with metabolic diseases. Therefore, excess sugar in plasma interferes with the functioning of IgG and may contribute to a wide range of diabetes-associated complications. The long-term formation of these heterogeneous AGEs may accumulate and affect plasma proteins, especially long-lived proteins. In this study, we analyze immunoglobulin-G (IgG) glycation with 2’-deoxyribose (deoxyribose) instigated modification in IgG structure and AGEs formation.

Methods: This study aims to glycate IgG from varying concentrations of pentose sugar, 2’-deoxyribose (deoxyribose). Various physicochemical methods and techniques characterized post glycation of IgG, both the native and its glycated analogue. The glycated protein will be assessed for its stability and perturbations by UV-VIS., fluorescence and FT-IR spectroscopic techniques. Moreover, the early glycation product will be done by NBT assay, and other biochemical parameters like HMF, carbonyl content and thioflavin-T assays were also performed to see the biochemical changes induced in the glycated IgG macromolecule.

Results: Glycation of protein macromolecules generates stable early glycation products (Amadori products). Later, these Amadori products involved a series of chemical reactions to form more stable advanced glycation end products (AGEs). Our experimental study results could validate the modification in IgG structure and AGEs formation.

Conclusion: The formation of IgG-AGEs from glycation of IgG with deoxyribose could exert cellular toxicity, and might initiates secondary complications of diabetes. Therefore, this study emphasized the glycation reaction of IgG from deoxyribose, which has not been reported yet.

Cite this article as:

Alenazi Fahaad*, Saleem Mohd, Syed Khaja Azharuddin Sajid, Zafar Mubashir, Alharbi Salem Mohammed, Hagbani Al Turki, Khan Yasir Mohd and Ahmad Saheem*, Glycation of Immunoglobulin-G from Pentose Sugar: A Cause for Structural Perturbations, Current Protein & Peptide Science 2022; 23 (11) . https://dx.doi.org/10.2174/1389203723666220929105859