Selective binding and dynamics of imidazole alkyl sulfate ionic liquids with human serum albumin and collagen – a detailed NMR investigation

2018 ◽  
Vol 20 (14) ◽  
pp. 9256-9268 ◽  
Author(s):  
R. Ravikanth Reddy ◽  
Ganesh Shanmugam ◽  
Balaraman Madhan ◽  
B. V. N. Phani Kumar
Keyword(s):  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spin Relaxation ◽  
Alkyl Sulfate ◽  
Binding Affinities ◽  
Selective Binding ◽  
Std Nmr ◽  
Anionic Part

STD NMR and selective spin-relaxation analysis evidenced the selective binding (anionic part) of imidazole alkyl sulfate ionic liquids with proteins (HSA and collagen). These studies also enabled the ionic liquids to be ranked based on their binding affinities with the proteins of study.

Effect of Ionic Liquids on the Solution Structure of Human Serum Albumin

2011 ◽  
Vol 12 (4) ◽  
pp. 1072-1079 ◽  
Author(s):  
Yasar Akdogan ◽  
Matthias J. N. Junk ◽  
Dariush Hinderberger
Keyword(s):  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solution Structure

Influence of Human Serum Albumin Glycation on the Binding Affinities for Natural Flavonoids

2019 ◽  
Vol 17 (1) ◽  
pp. 806-812
Author(s):  
Liangliang Liu ◽  
Yi Liu ◽  
Aiping Xiao ◽  
Shiyong Mei ◽  
Yixi Xie
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Small Molecules ◽  
Human Body ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Fluorescence Spectra ◽  
Binding Affinities ◽  
Dietary Flavonoids

AbstractIncreasing the degree of glycation in diabetes could affect the ability of plasma proteins in binding to small molecules and active compounds. In this study, the influence of glycation of Human serum albumin (HSA) on the binding affinities for six dietary flavonoids was investigated by fluorescence spectra. Glycated HSA was prepared through incubation with glucose and characterized by several methods to confirm the glycation. It was found that the level of glycation increased with the increasing incubation time. The glycation of HSA increased the binding affinities for flavonoids by 1.40 to 48.42 times, which indicates that modifications caused by the glycation may have different influences on the interactions of flavonoids with HSA at separate binding sites on this protein. These results are valuable for understanding the influence of diabetes on the metabolism of flavonoids and other bioactive small molecules in human body.

Human serum albumin-specific recognition of the natural herbal extract of Stryphnodendron polyphyllum through STD NMR, hyphenations and docking simulation studies

RSC Advances ◽  
2015 ◽  
Vol 5 (30) ◽  
pp. 23431-23442 ◽  
Author(s):  
Sheraz A. K. Tanoli ◽  
Nazish U. Tanoli ◽  
Tatiani M. Bondancia ◽  
Saman Usmani ◽  
Zaheer Ul-Haq ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Simulation ◽  
Herbal Extract ◽  
Rapid Screening ◽  
Simulation Studies ◽  
Specific Recognition ◽  
Screening And Identification ◽  
Std Nmr

Over the last two decades, new and more advanced strategies that help in the rapid screening and identification of new ligands for a specific macromolecule have become an important domain.

scholarly journals Unveiling the Interaction of Vanadium Compounds with Human Serum Albumin by Using1H STD NMR and Computational Docking Studies

2013 ◽  
Vol 2013 (26) ◽  
pp. 4619-4627 ◽  
Author(s):  
David M. Dias ◽  
João P. G. L. M. Rodrigues ◽  
Neuza S. Domingues ◽  
Alexandre M. J. J. Bonvin ◽  
M. Margarida C. A. Castro
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Studies ◽  
Vanadium Compounds ◽  
Computational Docking ◽  
Std Nmr

scholarly journals Insights into the Binding of Dietary Phenolic Compounds to Human Serum Albumin and Food-Drug Interactions

Pharmaceutics ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 1123
Author(s):  
Anallely López-Yerena ◽  
Maria Perez ◽  
Anna Vallverdú-Queralt ◽  
Elvira Escribano-Ferrer
Keyword(s):  
Phenolic Compounds ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Drug Interactions ◽  
Human Serum ◽  
Herbal Medicines ◽  
Drug Binding ◽  
Hydroxyl Groups ◽  
Binding Affinities ◽  
Native Form

The distribution of drugs and dietary phenolic compounds in the systemic circulation de-pends on, among other factors, unspecific/specific reversible binding to plasma proteins such as human serum albumin (HSA). Phenolic substances, present in plant-derived feeds, foods, beverages, herbal medicines, and dietary supplements, are of great interest due to their biological activity. Recently, considerable research has been directed at the formation of phenol–HSA complexes, focusing above all on structure–affinity relationships. The nucleophilicity and planarity of molecules can be altered by the number and position of hydroxyl groups on the aromatic ring and by hydrogenation. Binding affinities towards HSA may also differ between phenolic compounds in their native form and conjugates derived from phase II reactions. On the other hand, food–drug interactions may increase the concentration of free drugs in the blood, affecting their transport and/or disposition and in some cases provoking adverse or toxic effects. This is caused mainly by a decrease in drug binding affinities for HSA in the presence of flavonoids. Accordingly, to avoid the side effects arising from changes in plasma protein binding, the intake of flavonoid-rich food and beverages should be taken into consideration when treating certain pathologies.

Enantioselective binding of a lanthanide(iii) complex to human serum albumin studied by 1H STD NMR techniques

2011 ◽  
Vol 9 (14) ◽  
pp. 5047 ◽  
Author(s):  
David M. Dias ◽  
João M. C. Teixeira ◽  
Ilya Kuprov ◽  
Elizabeth J. New ◽  
David Parker ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nmr Techniques ◽  
Std Nmr
Sign in / Sign up

Export Citation Format

Share Document