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

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Computational prediction of interaction and pharmacokinetics profile study for polyamino-polycarboxylic ligands on binding with human serum albumin

New Journal of Chemistry ◽

10.1039/c9nj05594k ◽

2020 ◽

Vol 44 (7) ◽

pp. 2907-2918 ◽

Cited By ~ 1

Author(s):

Nidhi Chadha ◽

Dushyant Singh ◽

Marilyn D. Milton ◽

Gauri Mishra ◽

Joseph Daniel ◽

...

Keyword(s):

Fatty Acids ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Binding Sites ◽

Plasma Proteins ◽

Computational Prediction ◽

Profile Study ◽

Drugs And Metabolites

Human serum albumin (HSA) is one of the most abundant plasma proteins available in blood and responsible for transport of fatty acids, drugs and metabolites at its binding sites which are very important for the assessment of pharmacokinetics profile of the polyamino-polycarboxylic ligands.

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Zinc–human serum albumin association: testimony of two binding sites

Talanta ◽

10.1016/j.talanta.2003.10.054 ◽

2004 ◽

Vol 63 (2) ◽

pp. 503-508 ◽

Cited By ~ 21

Author(s):

C. André ◽

Y.C. Guillaume

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Binding Sites

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Metal-catalyzed oxidation of human serum albumin does not alter the interactive binding to the two principal drug binding sites

Biochemistry and Biophysics Reports ◽

10.1016/j.bbrep.2018.05.002 ◽

2018 ◽

Vol 14 ◽

pp. 155-160 ◽

Cited By ~ 1

Author(s):

Keishi Yamasaki ◽

Koji Nishi ◽

Makoto Anraku ◽

Kazuaki Taguchi ◽

Toru Maruyama ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Binding Sites ◽

Drug Binding ◽

Drug Binding Sites ◽

Metal Catalyzed Oxidation ◽

Metal Catalyzed ◽

Catalyzed Oxidation

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Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

JBIC Journal of Biological Inorganic Chemistry ◽

10.1007/s00775-012-0944-6 ◽

2012 ◽

Vol 18 (1) ◽

pp. 9-17 ◽

Cited By ~ 90

Author(s):

Orsolya Dömötör ◽

Christian G. Hartinger ◽

Anna K. Bytzek ◽

Tamás Kiss ◽

Bernhard K. Keppler ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Binding Sites

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Identifying Steroid Hormone Binding Sites on Human Serum Albumin by 2D NMR

Biophysical Journal ◽

10.1016/j.bpj.2012.11.2392 ◽

2013 ◽

Vol 104 (2) ◽

pp. 430a ◽

Cited By ~ 1

Author(s):

Eileen S. Krenzel ◽

Heidi A. Schwanz ◽

Ravi Jasu ◽

Michael Zakharov ◽

Shalendar Bhasin ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Binding Sites ◽

Steroid Hormone ◽

2D Nmr ◽

Hormone Binding

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Unique dynamic mode between Artepillin C and human serum albumin implies the characteristics of Brazilian green propolis representative bioactive component

Scientific Reports ◽

10.1038/s41598-020-74197-4 ◽

2020 ◽

Vol 10 (1) ◽

Author(s):

Fan Wu ◽

Xin-Mi Song ◽

Yi-Lei Qiu ◽

Huo-Qing Zheng ◽

Fu-Liang Hu ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Human Body ◽

Mode Interaction ◽

Dynamic Mode ◽

Bioactive Component ◽

Artepillin C ◽

Functional Components ◽

Brazilian Green Propolis

Abstract As a representative bioactive component in Brazil green propolis, Artepillin C (ArtC; 3, 5-diprenyl-4-hydroxycinnamic acid) has been reported a wide variety of physiological activities including anti-tumor, anti-inflammatory, and antimicrobial activity etc. However, it seems incompatible that ArtC in vivo was characterized as low absorption efficiency and low bioavailability. In order to obtain the elucidation, we further investigated the physicochemical basis of ArtC interacting with human serum albumin (HSA) in vitro. We found a unique dynamic mode interaction between ArtC and HSA, which is completely different from other reported propolis bioactive components. Thermodynamic analysis showed that hydrophobic interactions and electrostatic forces are the main driving force. The competitive assay indicates that the binding site of ArtC with HSA is close to the Sudlow’s site I. The findings of this study reveal the unique physicochemical transport mechanism of ArtC in the human body, which helps to further understand the uniqueness of the representative functional components of Brazilian green propolis in the human body.

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Indomethacin Increases Quercetin Affinity for Human Serum Albumin: A Combined Experimental and Computational Study and Its Broader Implications

International Journal of Molecular Sciences ◽

10.3390/ijms21165740 ◽

2020 ◽

Vol 21 (16) ◽

pp. 5740

Author(s):

Hrvoje Rimac ◽

Tana Tandarić ◽

Robert Vianello ◽

Mirza Bojić

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Binding Site ◽

Binding Sites ◽

Quantum Chemical ◽

Computational Study ◽

The Body ◽

Active Concentration ◽

Insight Into

Human serum albumin (HSA) is the most abundant carrier protein in the human body. Competition for the same binding site between different ligands can lead to an increased active concentration or a faster elimination of one or both ligands. Indomethacin and quercetin both bind to the binding site located in the IIA subdomain. To determine the nature of the HSA-indomethacin-quercetin interactions, spectrofluorometric, docking, molecular dynamics studies, and quantum chemical calculations were performed. The results show that the indomethacin and quercetin binding sites do not overlap. Moreover, the presence of quercetin does not influence the binding constant and position of indomethacin in the pocket. However, binding of quercetin is much more favorable in the presence of indomethacin, with its position and interactions with HSA significantly changed. These results provide a new insight into drug-drug interactions, which can be important in situations when displacement from HSA or other proteins is undesirable or even desirable. This principle could also be used to deliberately prolong or shorten the xenobiotics’ half-life in the body, depending on the desired outcomes.

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