Rhenium(I)-based fluorescence resonance energy transfer probe for conformational changes of bovine serum albumin

被引：26

作者：

Bhuvaneswari, Jayaraman ^{[1
]}

Fathima, Ayub Khan ^{[1
]}

Rajagopal, Seenivasan ^{[1
]}

机构：

[1] Madurai Kamaraj Univ, Sch Chem, Madurai 625021, Tamil Nadu, India

来源：

JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY | 2012年 / 227卷 / 01期

关键词：

Rhenium(I) tricarbonyl complex; Bovine serum albumin; Energy transfer; Protein binding; LOWEST EXCITED-STATE; CRYSTAL-STRUCTURE; RE(I) COMPLEXES; BINDING; PHOTOPHYSICS; CARBONYL; SITE;

D O I：

10.1016/j.jphotochem.2011.10.022

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Protein binding properties of fac-rhenium(I) complexes with general structure [Re(CO)(3)(N-N)L]PF6, where N-N = 4,4'-dinanoyl-2,2-bipyridine and L = py-3-COOH (la) and py-3-CONH2 (1b) with bovine serum albumin (BSA) were investigated at physiological pH (7.4) using UV-visible absorption and fluorescence spectral study, excited state lifetime measurement and circular dichroism (CD). The results observed from fluorescence spectra reveal the energy transfer from BSA to Re(I) complex, and the distance r between donor (BSA) and acceptor (Re(I) complex) is 3.05 nm and 2.16 nm for la and 1b respectively according to Forster's non-radiative energy transfer theory. CD results show that the binding of Re(I) complex could induce the conformational change with the loss of alpha-helicity. (C) 2011 Elsevier B.V. All rights reserved.

引用

页码：38 / 44

页数：7

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