Spectrometry researches on interaction and sonodynamic damage of riboflavin (RF) to bovine serum albumin (BSA)
| Autor: | Ying Li, Yumei Kong, Zhiqiu Wang, Lixin Xia, Jun Wang, Siyu Wang, Mingming Zou, Jushi Li |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Radical
Riboflavin Serum albumin Photochemistry Analytical Chemistry chemistry.chemical_compound Animals Ultrasonics Bovine serum albumin Instrumentation Spectroscopy chemistry.chemical_classification Reactive oxygen species Aqueous solution biology Chemistry Singlet oxygen Tryptophan Serum Albumin Bovine Fluorescence Atomic and Molecular Physics and Optics Spectrometry Fluorescence biology.protein Cattle Spectrophotometry Ultraviolet Reactive Oxygen Species Nuclear chemistry Protein Binding |
| Zdroj: | Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy. 87 |
| ISSN: | 1873-3557 |
| Popis: | In this paper, the riboflavin (RF) was used to study the interaction and sonodynamic damage to bovine serum albumin (BSA) by fluorescence and UV-vis spectroscopy. The results showed that the RF could efficiently bind to BSA in aqueous solution. Under ultrasonic irradiation, the RF could obviously damage the BSA. In addition, synchronous fluorescence spectroscopy revealed that the RF showed more accessible to tryptophan (Trp) residues than to tyrosine (Tyr) residues. Also, it damaged Trp residues more seriously than Tyr residues under ultrasonic irradiation. At last, the generation of reactive oxygen species (ROS) in sonodynamic process was estimated by the method of Oxidation-Extraction Spectrometry (OES). And then, several radical scavengers were used to determine the kind of ROS. It was found that at least the singlet oxygen ((1)O(2)) and hydroxyl radicals (*OH) were generated. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect