Conjugation of a Dipicolyl Chelate to Polypeptide Conjugates Increases Binding Affinities for Human Serum Albumin and Survival Times in Human Serum

ChemBioChem ◽  
2017 ◽  
Vol 18 (14) ◽  
pp. 1408-1414 ◽  
Author(s):  
Aleksandra Balliu ◽  
Lars Baltzer
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinities ◽  
Survival Times

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.

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.

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.

scholarly journals Cheminformatic Models To Predict Binding Affinities to Human Serum Albumin

2001 ◽  
Vol 44 (25) ◽  
pp. 4370-4378 ◽  
Author(s):  
Gonzalo Colmenarejo ◽  
Ana Alvarez-Pedraglio ◽  
José-Luis Lavandera
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinities

Investigating the binding affinities of fructose and galactose to human serum albumin: simulation studies

2021 ◽  
pp. 1-10
Author(s):  
Tadsanee Awang ◽  
Jitti Niramitranon ◽  
Deanpen Japrung ◽  
Patchreenart Saparpakorn ◽  
Prapasiri Pongprayoon
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinities ◽  
Simulation Studies
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