Glycation of human serum albumin alters its binding efficacy towards the dietary polyphenols: a comparative approach

Abstract

Diabetes is a major problem in the world. The proteins became modified during glycation after reacting with the reducing sugars (e.g. D-glucose) via non-enzymatic pathways. The glycated analogue of human serum albumin (HSA) has been characterized with the help of multi-spectroscopic methods. It has been observed that six glucose molecules can bind covalently to HSA under experimental condition. The binding affinity of the modified HSA towards the dietary polyphenols has been estimated using UV-vis and fluorescence spectroscopic techniques. The binding constant values of the ligands were found to decrease after the modification of HSA.

Non-enzymatic glycation of human serum albumin modulates its binding efficacy towards bioactive flavonoid chrysin: A detailed study using multi-spectroscopic and computational methods

“…The Trp fluorescence intensity of the modified HSA was found lower than that of the native HSA. Similar observation was also reported earlier by Roy et al and Coussons et al(Coussons et al 1997;Singha Roy, Ghosh & Dasgupta 2016)…”

“…The absorbance of the glycated sample was found out to be more than its native form as shown in the Figure S1. Similar observation was reported by Roy et al (Singha Roy, Ghosh & Dasgupta 2016). A visible browning of the glycated sample was also noticed.…”

“…to the partial unfolding of HSA during glycation. Similar observations were reported by Roy et al for the glycation of HSA(Singha Roy et al 2016). …”

Binding of Plant Polyphenols to Serum Albumin and LDL: Healthy Implications for Heart Disease

“…Thus, binding of PP to HSA in a physiological matrix is both protective for HSA as well as indirectly LDL and HDL. PP binding to HSA inhibits its aggregation as well as glycation (hyperglycemia conditions), which induces aggregation . Moreover PP–protein binding in blood at physiological concentrations inhibits platelet aggregation, an important cardiovascular benefit …”

“…PP binding to HSA inhibits its aggregation as well as glycation (hyperglycemia conditions), which induces aggregation. 43 Moreover PP−protein binding in blood at physiological concentrations inhibits platelet aggregation, an important cardiovascular benefit. 44 The first indirect example of binding of PP to LDL was in 1995.…”