Inhibitory effect of quercetin in the formation of advance glycation end products of human serum albumin: An in vitro and molecular interaction study

2015 ◽  
Vol 79 ◽  
pp. 336-343 ◽  
Author(s):  
Md. Maroof Alam ◽  
Irshad Ahmad ◽  
Imrana Naseem
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Interaction ◽  
Inhibitory Effect ◽  
Interaction Study ◽  
Glycation End Products ◽  
End Products

Systematical investigation of in vitro molecular interaction between fluorescent carbon dots and human serum albumin

RSC Advances ◽  
2016 ◽  
Vol 6 (50) ◽  
pp. 44531-44542 ◽  
Author(s):  
Shan Huang ◽  
Hangna Qiu ◽  
Jiangning Xie ◽  
Chusheng Huang ◽  
Wei Su ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Interaction ◽  
Carbon Dots ◽  
Electrochemical Techniques ◽  
Fluorescent Carbon Dots ◽  
Fluorescent Carbon

In vitro molecular interaction between fluorescent CDs and HSA was systematically investigated by multispectroscopic and electrochemical techniques.

scholarly journals In-vitro molecular interaction of boron doped carbon dots with human serum albumin

2021 ◽  
Vol 1120 (1) ◽  
pp. 012012
Author(s):  
Vinayak Sahu ◽  
Fahmida Khan ◽  
Pradeep Kumar Dewangan ◽  
Komal Kashyap ◽  
Sonalika Agrawal ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Interaction ◽  
Carbon Dots ◽  
Boron Doped ◽  
Doped Carbon Dots

scholarly journals A Biophysical Comparison of Human Serum Albumin to be Glycated In Vivo and In Vitro

2011 ◽  
Vol 30 (1) ◽  
pp. 5-10 ◽  
Author(s):  
Naghmeh Sattarahmady ◽  
Ali Moosavi-Movahedi ◽  
Mehran Habibi-Rezaei
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Physiological Conditions ◽  
Glycation End Products ◽  
Biophysical Studies ◽  
Arginine Residues ◽  
Glycation Process

A Biophysical Comparison of Human Serum Albumin to be GlycatedIn VivoandIn VitroThe glycation process includes the arrangement of proteins with chemically reversible early glycation products, Schiff bases and Amadori adducts. These early products endure slow and complex rearrangements to create advanced glycation end-products (AGEs) that are involved in diabetic complications. Here, the biophysical characteristics ofin vitroglycated human serum albumin (HSA) are compared to those of HSA glycatedin vivo. The changes in the content of α-helices, AGE-specific fluorescence intensity, extent of lysine residue modification, and surface tension value and also the formation of Amadori products in HSA are similar in both conditions. It was observed, however, that arginine residues were modified only under physiological conditions (in vivo), while the same did not occurin vitro. This difference was related to the presence of 3-deoxyglucosone, a 1,2-dicarbonyl compound derived from glucose under physiological conditions. Therefore, the biophysical studies on the HSA glycation processin vitroare credible.

Inhibition of fluorescent advanced glycation end products (AGEs) of human serum albumin upon incubation with 3-β-hydroxybutyrate

2014 ◽  
Vol 41 (6) ◽  
pp. 3705-3713 ◽  
Author(s):  
M. Bohlooli ◽  
A. A. Moosavi-Movahedi ◽  
F. Taghavi ◽  
A. A. Saboury ◽  
P. Maghami ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Advanced Glycation End Products ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products
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