Study of the interaction between CdSe/ZnS core-shell quantum dots and bovine serum albumin by spectroscopic techniques

被引：60

作者：

Dzagli, Milohum Mikesokpo ^{[1
,2
,3
]}

Canpean, Valentin ^{[1
,2
]}

Iosin, Monica ^{[1
,2
]}

Mohou, Messanh Agbeko ^{[3
]}

Astilean, Simion ^{[1
,2
]}

机构：

[1] Univ Babes Bolyai, Fac Phys, Cluj Napoca 400271, Romania

[2] Nanobiophoton Ctr, Inst Interdisciplinary Expt Res Bionanosci, Cluj Napoca 400271, Romania

[3] Univ Lome, Lab Phys Composants Semicond, Lome, Togo

来源：

JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY | 2010年 / 215卷 / 01期

关键词：

Quantum dots; Bovine serum albumin; Quenching; Fluorescence; Biosensing; GOLD NANOPARTICLES; TEMPERATURE; PHOTOLUMINESCENCE; STOICHIOMETRY; BINDING; CELLS;

D O I：

10.1016/j.jphotochem.2010.08.008

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：

In this work we studied the interaction between CdSe/ZnS core-shell quantum dots (QDs) and bovine serum albumin (BSA) protein, and the temperature effects on the structural and spectroscopic properties of both, individual QDs and protein and their bioconjugates (QDs@BSA), by fluorescence and UV-vis spectroscopy. The recorded UV-vis data and the calculated rate of BSA fluorescence quenching by the QDs demonstrated that the interaction between them leads to the formation of QDs@BSA complex. Moreover we show that, compared to the monotonically decrease of the non-conjugated QDs fluorescence intensity, the temperature dependence of the QDs@BSA emission has a much more complex behavior, highly sensitive to the conformational changes of the protein. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：118 / 122

页数：5

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