NDLI: Binding Citrus flavanones to human serum albumin: effect of structure on affinity

Content Provider	Springer Nature Link
Author	Cao, Hui Chen, Longsheng Xiao, Jianbo
Copyright Year	2010
Abstract	Much of the bioactivities of Citrus flavanones significantly appear to impact blood and microvascular endothelial cells. It is essential to investigate the interaction between Citrus flavanones and serum albumin to verify the effect of flavanone structures on the distribution and transportation in blood. The interactions between flavonoids and proteins have attracted great interest among researchers. The work in here mainly concerns about the binding interaction between Citrus flavanones and human serum albumin (HSA) in vitro. The methoxylation of tangeretin improved the affinity for HSA by 100 times. The 2,3-double bond in conjugation with a 4-oxo group plays an important role for the affinity for HSA. The affinity of apigenin for HSA is about 10,000-times higher than that of naringenin. It was found that the hydroxylation on position 3′ of flavonol significantly improves the binding affinity for HSA. The affinity of quercetin (3′, 4′) for HSA is about 100-times higher than that of kaempferol (4′). The hydroxylation on position 3′ of flavone slightly improves the binding affinity for HSA. The affinity of luteolin for HSA is about 1.38-times higher than that of apigenin. The values of log$_{10}$(K$_{a}$) are proportional to the number of binding sites (n), which confirms the method used here is suitable to study the interaction between Citrus flavanones and HSA.
Starting Page	2257
Ending Page	2262
Page Count	6
File Format	PDF
ISSN	03014851
Journal	Molecular Biology Reports
Volume Number	38
Issue Number	4
e-ISSN	15734978
Language	English
Publisher	Springer Netherlands
Publisher Date	2010-09-29
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Citrus flavanones Affinity HSA Naringenin Naringin Narirutin Nobiletin Tangeretin Animal Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Genetics Medicine Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The Binding of Benzopyranes to Human Serum Albumin. A Structure–Affinity Study

The specific binding of chlorogenic acid to human serum albumin

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Study on the interaction of a copper(II) complex containing the artificial sweetener aspartame with human serum albumin

Evaluation of binding and thermodynamic characteristics of interactions between a citrus flavonoid hesperitin with protein and effects of metal ions on binding

Binding of berberine to bovine serum albumin: spectroscopic approach

Binding properties of food colorant allura red with human serum albumin in vitro

Crystal Structure Analysis of Warfarin Binding to Human Serum Albumin ANATOMY OF DRUG SITE I

Interaction of human serum albumin with 10-hydroxycamptothecin: spectroscopic and molecular modeling studies

Binding Citrus flavanones to human serum albumin: effect of structure on affinity

Similar Documents

The Binding of Benzopyranes to Human Serum Albumin. A Structure–Affinity Study

The specific binding of chlorogenic acid to human serum albumin

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Study on the interaction of a copper(II) complex containing the artificial sweetener aspartame with human serum albumin

Evaluation of binding and thermodynamic characteristics of interactions between a citrus flavonoid hesperitin with protein and effects of metal ions on binding

Binding of berberine to bovine serum albumin: spectroscopic approach

Binding properties of food colorant allura red with human serum albumin in vitro

Crystal Structure Analysis of Warfarin Binding to Human Serum Albumin ANATOMY OF DRUG SITE I

Interaction of human serum albumin with 10-hydroxycamptothecin: spectroscopic and molecular modeling studies

Binding Citrus flavanones to human serum albumin: effect of structure on affinity