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Current Pharmaceutical Biotechnology

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ISSN (Print): 1389-2010
ISSN (Online): 1873-4316

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Research Article

Glyoxal Induced Transition of Transferrin to Aggregates: Spectroscopic, Microscopic and Molecular Docking Insight

Author(s): Anas Shamsi, Khan M. Abdullah, Hina Usmani, Areeba Shahab, Hamza Hasan and Imrana Naseem*

Volume 20, Issue 12, 2019

Page: [1028 - 1036] Pages: 9

DOI: 10.2174/1389201020666190731122806

Price: $65

Abstract

Background & Objective: The present study was aimed at characterizing the conformational alterations induced in human transferrin, the iron regulatory protein by glyoxal. Since protein aggregation is at the core of many disorders, thus interest in this domain has increased significantly during the past years.

Methods: In our present study, the effect of glyoxal was monitored on human transferrin using multispectroscopic and multi-microscopic studies.

Results: Intrinsic fluorescence spectroscopy suggested changes in native conformation of human transferrin evident by decreased fluorescence and blue shift in the presence of glyoxal. Further, extrinsic fluorescence was retorted and the results showed the formation of aggregates; apparent by increased Congo red (CR) absorbance, Thioflavin T (ThT) and ANS fluorescence and TEM of human transferrin in the presence of glyoxal. Molecular docking was also employed to see which residues are at core of human transferrin and glyoxal interaction. Reactive oxygen species (ROS) generation assays revealed enhanced ROS levels by human transferrin after treatment with glyoxal.

Conclusion: Thus, our study proposes that glyoxal induces the formation of aggregates in human transferrin. These aggregates further generate ROS which are key players in the complications associated with diabetes mellitus, giving our study clinical perspective.

Keywords: Human transferrin, spectroscopy, microscopy, molecular docking, reactive oxygen species, glyoxal.

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