Surface-enhanced Raman scattering studies on the recognition mechanism of glutathione peroxidase mimics, bis-cyclodextrin diselenide
Surface-enhanced Raman scattering studies on the recognition mechanism of glutathione peroxidase mimics, bis-cyclodextrin diselenide
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表面增强拉曼散射研究谷胱甘肽过氧化物酶模拟物双环糊精二硒化物的识别机制
DOI:
10.1016/j.colsurfa.2004.10.035
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发表时间:
2005-05-05
影响因子:
5.2
通讯作者:
Luo, GM
中科院分区:
文献类型:
--
作者:
Hao, YQ;Wu, YQ;Luo, GM
Surface-enhanced Raman scattering (SERS) spectroscopy has been used to explore the recognition mechanism between a selenium-containing glutathione peroxidase (GPX) mimic, 2,2'-diseleno-bis-p-cyclodextrin (2-SeCD) and two glutathione (GSH) alternatives, S-dinitrophenyl-glutathione (GSH-S-DNP) and 4,4'-bis(carboxymethyleneoxy)azobenzene (BCMAB). SERS spectra have been employed to investigate how these alternatives bind with beta-CD and 2-SeCD. SERS signals of the spectra of GSH-S-DNP and BCMAB are much intense ill comparison with those of theirs complexes, GSH-S-DNP/CDs and BCMAB/CDs in silver colloid solutions, which suggest that GSH-S-DNP and BCMAB are included into the CD cavity when they bind with beta-CD or 2-SeCD. Weak Raman signals in the SERS spectra of the GSH-S-DNP/CDs in silver colloid solution make it difficult to investigate the recognition mechanism between CDs and GSH-S-DNP by using SERS efficiently. The bands at 1388 and 1379 cm(-1) in the SERS spectra of BCMAB/CDs strongly suggest that BCMAB does not bind with beta-CD or 2-SeCD via its -COOH group. (c) 2004 Elsevier B.V. All rights reserved.