Journal
SCIENCE OF THE TOTAL ENVIRONMENT
Volume 407, Issue 18, Pages 5019-5023Publisher
ELSEVIER
DOI: 10.1016/j.scitotenv.2009.05.052
Keywords
CdTe quantum dots; Bovine serum albumin; Fluorescence spectra
Categories
Funding
- 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]
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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.
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