Health & Environmental Research Online (HERO)


Print Feedback Export to File
7681761 
Journal Article 
Interactions of Pyrene with Human Serum Albumin and Bovine Serum Albumin: Microenvironmental Polarity Differences at Binding Sites 
Li Mengshuo; Zhang Jing; Liu Dan; Zhu Yaxian; Zhang Yong 
2021 
1 
Gaodeng Xuexiao Huaxue Xuebao / Chemical Journal of Chinese Universities
ISSN: 0251-0790 
Higher Education Press Limited Company 
42 
3 
731-735 
Chinese 
WOS:000627118700008 
The interactions of pyrene(Pyr), a microenvironmental hydrophobic fluorescent probe, with human serum albumin(HSA) or bovine serum albumin(BSA) were investigated using steady-state fluorescence, fluorescence resonance energy transfer technology, and molecular docking methods. It was observed that the average values of I1/I3 of the Pyr in the presence of HSA or BSA are 1.36 and 0.92, respectively. The binding constants of Pyr with HSA or BSA has been decreased from 1.86×107 L/mol to 1.71×105 L/mol. The apparent distances of Pyr to tryptophan residues in HSA or BSA were calculated to be 2.37 and 2.34 nm. The binding sites of Pyr in HSA or BSA were located in subdomain ⅠB and subdomains ⅠA, respectively. The polarity of amino acid residues around the binding sites was one of the main factors affecting the I1/I3 value of Pyr. The experimental results suggested that there were significant differences in the binding sites and its microenvironmental polarity of BSA and HSA with Pyr. © 2021, Editorial Department of Chem. J. Chinese Universities. All right reserved. 
Pyrene; Human serum albumin; Bovine serum albumin; Microenvironmental polarity; Interaction mechanism