Interaction of different thiol-capped CdTe quantum dots with bovine serum albumin
| Autor: | Pengfei Liu, Xinmin Min, Xiaolei Zhang, Peng Liu, Tingting Fang, Qisui Wang, Xiaolan Zhou, Xi Li |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Quenching
Circular dichroism Conformational change biology Chemistry technology industry and agriculture Biophysics General Chemistry equipment and supplies Condensed Matter Physics Ligand (biochemistry) Biochemistry Fluorescence Atomic and Molecular Physics and Optics Crystallography Quantum dot biology.protein Absorption (chemistry) Bovine serum albumin |
| Zdroj: | Journal of Luminescence. 132:1695-1700 |
| ISSN: | 0022-2313 |
| DOI: | 10.1016/j.jlumin.2012.02.016 |
| Popis: | Due to their unique optical properties, quantum dots (QDs) are rapidly revolutionizing many areas of medicine and biology. Despite the remarkable speed of development of nanoscience, relatively little is known about the interaction of nanoscale objects with organism. In this work, interaction of CdTe QDs coated with mercaptopropanoic acid (MPA), L-cysteine (L-cys), and glutathione (GSH) with bovine serum albumin (BSA) was investigated. Fluorescence (FL), UV–vis absorption, and circular dichroism (CD) spectra methods were used. The Stern-Volmer quenching constant (Ksv) at different temperatures, corresponding thermodynamic parameters (ΔH, ΔG and ΔS), and information of the structural features of BSA were gained. We found that QDs can effectively quench the FL of BSA in a ligand-dependent manner, electrostatic interactions play a major role in the binding reaction, and the nature of quenching is static, resulting in forming QDs-BSA complexes. The CD spectra showed that the secondary and tertiary structure of BSA was changed. This study contributes to a better understanding of the ligand effects on QDs-proteins interactions, which is a critical issue for the applications in vivo. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect