Issue 19, 2012
From the journal:

RSC Advances

MC-LR@HSA: non-covalent interaction and effect†

Chao Song,a   Yan-Qin Zib  and  Hong-Wen Gao*a  

* Corresponding authors

a State Key Laboratory of Pollution Control and Resource Reuse, College of Environmental Science and Engineering, Tongji University, Shanghai, China
E-mail: EMSL@tongji.edu.cn
Fax: (+)86-21-6598-8598

b School of Chemistry & Materials, Huaibei Normal University, Anhui, China

Abstract

Three microcystin-LR molecules binding to subdomains IA, IIA, IIIA and IIB of human serum albumin (HSA) via hydrophobic interaction and hydrogen bonding induced the HSA conformation to transfer from α-helix to β-pleated sheet and random coils so that HSA transport of vitamin B2 was inhibited.

Graphical abstract: MC-LR@HSA: non-covalent interaction and effect

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Article information

DOI
https://doi.org/10.1039/C2RA20874A
Article type
Communication
Submitted
07 May 2012
Accepted
25 Jun 2012
First published
26 Jun 2012

RSC Adv., 2012,2, 7400-7402

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MC-LR@HSA: non-covalent interaction and effect

C. Song, Y. Zi and H. Gao, RSC Adv., 2012, 2, 7400 DOI: 10.1039/C2RA20874A

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