Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex-Reference-Cited by-同舟云学术

Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex

Published:2015 Issue:8 Volume:6 Page:2712-2726
ISSN:2042-6496
Container-title:Food & Function
language:en
Short-container-title:Food Funct.

Author:

Peng Xin¹²³⁴⁵,Wang Xiangchao⁵⁶²³⁴,Qi Wei⁵⁶²³⁴,Huang Renliang⁷²³⁴,Su Rongxin⁵⁶²³⁴,He Zhimin⁵⁶²³⁴

Affiliation:

1. School of Life Sciences

2. Tianjin University

3. Tianjin 300072

4. PR China

5. Chemical Engineering Research Center

6. School of Chemical Engineering and Technology

7. School of Environmental Science and Engineering

Abstract

Rosmarinic acid (RA) is an importantly and naturally occurring polyphenol. The interaction between bovine serum albumin and rosmarinic acid was studied to investigate the binding patterns and conformation changes.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Medicine,Food Science

Link

http://pubs.rsc.org/en/content/articlepdf/2015/FO/C5FO00597C

Reference60 articles.

1. Dietary phenolics: chemistry, bioavailability and effects on health

2. Rosmarinic acid: new aspects

3. Effects of rosmarinic acid on liver and kidney antioxidant enzymes, lipid peroxidation and tissue ultrastructure in aging mice

4. Rosmarinic Acid Extract for Antioxidant, Antiallergic, and α-Glucosidase Inhibitory Activities, Isolated by Supramolecular Technique and Solvent Extraction from Perilla Leaves

5. Absorption, metabolism, degradation and urinary excretion of rosmarinic acid after intake of Perilla frutescens extract in humans

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