Details

Autor(en) / Beteiligte

• Shen, Yizhong
• Zhu, Chunlei
• Wang, Yaping
• Xu, Jingjing
• Xue, Ruyu
• Ji, Fuyun
• Wu, Yiwei
• Wu, Zeyu
• Zhang, Wencheng
• Zheng, Zhi
• Ye, Yingwang

Titel

Evaluation the binding of chelerythrine, a potentially harmful toxin, with bovine serum albumin

Ist Teil von

• Food and chemical toxicology, 2020-01, Vol.135, p.110933-110933, Article 110933

Ort / Verlag

England: Elsevier Ltd

Erscheinungsjahr

2020

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Chelerythrine (CHE), a benzophenanthridine alkaloid, is usually used as a nutritional and functional additive in variety of health foods. However, it should be paid enough attention because of its potential toxicity to human health. In this work, the binding mechanism of CHE with bovine serum albumin (BSA) was systematically investigated with spectroscopic approaches. The results showed that the mixture of BSA with CHE could spontaneously cause the formation of BSA-CHE complex through electrostatic interaction under simulative physiological conditions (0.01 mol L−1 Tris-HCl, 0.015 mol L−1 NaCl, pH = 7.4). Site marker competitive displacement experiments exhibited that CHE was primarily bound to the hydrophobic pocket of the site II (subdomain IIIA) of BSA. It has been reported that the binding of small functional molecules to serum albumins remarkably impacts their absorption, distribution, metabolism, conformation, and excretion features. Therefore, this study might be helpful for human to have an in-depth understanding of the biological effect of CHE in vivo and guide human to take it safely and reasonably. •Exploring the interaction mechanism of CHE to BSA by spectroscopic approaches.•Revealing CHE primarily binds to the site II (subdomain IIIA) of BSA.•Helping us apprehend the transportation mechanism and toxicity of CHE in vivo.