Investigation on the binding of cyanobacterial metabolite calothrixin A with human serum albumin for evaluating its potential toxicology. (September 2021)

• Record Type: Journal Article
• Authors: Liao, Xianjiu; Zhu, Chunlei; Zhang, Haiyan; Li, Xuemin; Wen, Xiaoqing; Zhang, Shao-Lin; Shen, Yizhong
• Is Part Of: Food and chemical toxicology. Volume 155(2021)
• Publication Date: 2021-09
• Subjects: Calothrixin A -- Human serum albumin -- Toxicology -- Multi-spectroscopies -- Molecular docking; Toxicology -- Periodicals; Food poisoning -- Periodicals; Food Poisoning -- Periodicals; Toxicology -- Periodicals; Toxicologie -- Périodiques; Intoxications alimentaires -- Périodiques; Food poisoning; Toxicology; Periodicals; Electronic journals; 615.9
• DOI: 10.1016/j.fct.2021.112396
• Languages: English
• ISSNs: 0278-6915

Abstract

Abstract: Calothrixin A (CLA ), as a carbazole-1, 4-quinone alkaloid with unique indolo [3, 2- j ] phenanthridine framework, is a natural metabolite from the Calothrix cyanobacteria . Since the interaction to the functional serum albumins may play an important role in estimating its potential physiological or toxicological effects in vivo, we here explored the binding information of CLA with human serum albumin (HSA) by multi-spectroscopic experiments and computational approaches. The molecular docking results showed that there was one binding site of CLA to the site I (subdomain IIA) of HSA, causing the spontaneous formation of the ground state complex of CLA -HSA through the integration of hydrogen bond, hydrophobic interaction, and electrostatic interaction. Moreover, CLA could effectively trigger the change of HSA's secondary structure because of an obvious decrease of α-helical content in HSA. Taking into consideration of the crucial role of HSA to transport extraneous functional small molecules in vivo, this study may provide a worthy theoretical basis to evaluate the in vivo toxicity of CLA, aiming to reduce/avoid the potential toxic side effects of CLA in the next hit-to-lead campaign. Highlights: The binding information of CLA to HSA was investigated by spectroscopic and molecular docking methods. CLA bound to HSA primary via hydrogen bond, hydrophobic interaction, and electrostatic interaction. CLA induced an obvious variation in the conformation structure of HSA. Attempting to study the potential toxicology of CLA through its binding with HSA.