期刊
SCIENCE OF THE TOTAL ENVIRONMENT
卷 407, 期 18, 页码 5019-5023出版社
ELSEVIER
DOI: 10.1016/j.scitotenv.2009.05.052
关键词
CdTe quantum dots; Bovine serum albumin; Fluorescence spectra
资金
- NSFC [20607011, 20875055]
- Ministry of Education of China [708058, NCET-06-0582]
- Foundation for Middle Young Scientists
- Key Science-Technology Project in Shandong Province [2007BS08005, 2008GG10006012]
The biological toxicity of CdTe quantum dots (QDs) to bovine serum albumin (BSA) has been investigated mainly by fluorescence spectra, UV-vis absorption spectra and circular dichroism (CD) under simulative physiological conditions. Fluorescence data revealed that the quenching mechanism of BSA by CdTe QDs was a static quenching process and the binding constant is 6.05 x 10(3) and the number of binding sites is 0.7938. The thermodynamic parameters (Delta H = -62.33 kJ mol(-1). Delta G = -21.21 kJ mol(-1), and Delta S = -140.3 J mol(-1) s(-1)) indicate that hydrogen bonds and van der Waals forces between the protein and the QDs are the main binding forces stabilizing the complex. In addition, UV-vis and CD results showed that the addition of CdTe QDs changed the conformation of BSA. (C) 2009 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据