title: New strategy for the evaluation of CdTe quantum dot toxicity targeted to bovine serum albumin.
abstract: 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 6.05x10(3) and the number of binding sites is 0.7938. The thermodynamic parameters (DeltaH=-62.33 kJ mol(-1), DeltaG=-21.21 kJ mol(-1), and DeltaS=-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.
authors.affiliation: School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan 250100, PR China.
authors.forename: Lingzi
authors.initials: L
authors.lastname: Zhao
authors.forename: Rutao
authors.initials: R
authors.lastname: Liu
authors.forename: Xingchen
authors.initials: X
authors.lastname: Zhao
authors.forename: Bingjun
authors.initials: B
authors.lastname: Yang
authors.forename: Canzhu
authors.initials: C
authors.lastname: Gao
authors.forename: Xiaopeng
authors.initials: X
authors.lastname: Hao
authors.forename: Yongzhong
authors.initials: Y
authors.lastname: Wu
mesh_terms: D019187:Cadmium Compounds / Q000633:toxicity*; D002942:Circular Dichroism; D006860:Hydrogen Bonding; D011487:Protein Conformation; D045663:Quantum Dots; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000187:drug effects*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013691:Tellurium / Q000633:toxicity*; D013816:Thermodynamics
chemical_list: D019187:Cadmium Compounds; D012710:Serum Albumin, Bovine; D013691:Tellurium; C028337:cadmium telluride