Glyoxal induced transition of transferrin to aggregates: Spectroscopic, microscopic and molecular docking insight.

Glyoxal induced transition of transferrin to aggregates: Spectroscopic, microscopic and molecular docking insight.
Curr Pharm Biotechnol. 2019 Jul 31;:
Authors: Shamsi A, Abdullah KM, Usmani H, Shahab A, Hasan H, Naseem I
Abstract
The present study was aimed at characterizing the conformational alterations induced in human transferrin (hTF), the iron regulatory protein by glyoxal. Since, protein aggregation is at core of many disorders, thus interest in this domain has increased significantly during past years. In our present study, effect of glyoxal was monitored on hTF using multispectroscopic and multi-microscopic studies. Intrinsic fluorescence spectroscopy suggested transition of native hTF towards non-native form. Further, extrinsic fluorescence was retorted and the results were suggestive of this non-native form to be aggregates which is evident by increased ANS and ThT fluorescence of hTF. SEM evaluation revealed globular nature of these aggregates. Molecular docking was done to have an insight into the binding of hTF and glyoxal. ROS generation assays revealed significant generation by these aggregates as evident from enhanced ROS levels by hTF after treatment with glyoxal. Thus, we proposed that glyoxal induces the formation of aggregates in hTF. These aggregates generate ROS which are key players in the complications associated to diabetes mellitus, giving our study clinical perspective.
PMID: 31364512 [PubMed - as...

Source: Current Pharmaceutical Biotechnology - July 30, 2019 Category: Biotechnology Authors: Shamsi A, Abdullah KM, Usmani H, Shahab A, Hasan H, Naseem I Tags: Curr Pharm Biotechnol Source Type: research