Issue 2, 2012
From the journal:

RSC Advances

The adsorption of an anticancer hydrazone by protein: an unusual static quenching mechanism†

Fang-Fang Tian,a   Jia-Han Li,a   Feng-Lei Jiang,a   Xiao-Le Han,a   Chen Xiang,a   Yu-Shu Ge,a   Li-Li Lia  and  Yi Liu*a  

* Corresponding authors

a State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for Biology and Medicine (MOE), College of Chemistry and Molecular Sciences, Wuhan University, Wuhan, P. R. China
E-mail: yiliuchem@whu.edu.cn
Fax: +86 27 68756667

Abstract

A novel hydrazone, 4-chloro-N′-(pyridin-2-ylmethylene)benzohydrazide (CPBH) has been synthesized through a one-pot synthesis method and used as a chemical probe to find the structural cause of the unusual static quenching mechanism in the interaction with serum albumin. The adsorption of CPBH by bovine/human serum albumin (BSA/HSA) has been investigated systematically by comprehensive spectroscopy, modeling, electrochemistry and microcalorimetry under physiological conditions. CPBH forms a complex with BSA/HSA with the binding site in Sudlow's site I of BSA/HSA. The adverse temperature dependence in the unusual static quenching is found to be a reasonable consequence of the large activation energy requirement in the binding process, which is required to overcome the structural block and it is a direct result of the unique microstructure of the binding pocket.

Graphical abstract: The adsorption of an anticancer hydrazone by protein: an unusual static quenching mechanism

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Article information

DOI
https://doi.org/10.1039/C1RA00521A
Article type
Paper
Submitted
27 Jul 2011
Accepted
27 Sep 2011
First published
16 Nov 2011

RSC Adv., 2012,2, 501-513

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The adsorption of an anticancer hydrazone by protein: an unusual static quenching mechanism

F. Tian, J. Li, F. Jiang, X. Han, C. Xiang, Y. Ge, L. Li and Y. Liu, RSC Adv., 2012, 2, 501 DOI: 10.1039/C1RA00521A

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