New insight into the binding interaction of hydroxylated carbon nanotubes with bovine serum albumin
| Autor: | Hongmei Zhang, Yonghui Guan, Yanqing Wang |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Protein Denaturation
Circular dichroism Carbon nanotube Hydroxylation Protein Structure Secondary Fluorescence spectroscopy Analytical Chemistry law.invention Protein Aggregates law Animals Molecule Organic chemistry Denaturation (biochemistry) Benzothiazoles Bovine serum albumin Instrumentation Protein secondary structure Guanidine Spectroscopy biology Nanotubes Carbon Chemistry Circular Dichroism Serum Albumin Bovine Hydrogen-Ion Concentration Atomic and Molecular Physics and Optics Molecular Docking Simulation Kinetics Thiazoles Fluorescence intensity Spectrometry Fluorescence biology.protein Biophysics Cattle Protein Binding |
| Zdroj: | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 124:556-563 |
| ISSN: | 1386-1425 |
| DOI: | 10.1016/j.saa.2014.01.058 |
| Popis: | In order to understand the effects of carbon nanotubes on the structural stability of proteins, the ligand-binding ability, fibrillation, and chemical denaturation of bovine serum albumin in the presence of a multi-walled hydroxylated carbon nanotubes (HO-MWCNTs) was characterized by UV–vis, circular dichroism, fluorescence spectroscopy and molecule modeling methods at the molecular level. The experiment results indicated that the fluorescence intensity of BSA was decreased obviously in presence of HO-MWCNTs. The binding interaction of HO-MWCNTs with BSA led to the secondary structure changes of BSA. This interaction could not only affect the ligand-binding ability of BSA, but also change the rate of fibrillation and denaturation of BSA. This work gave us some important information about the structures and properties of protein induced by carbon nanotubes. |
| Databáze: | OpenAIRE |
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