刊名:Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
出版年:2017
出版时间:15 February 2017
年:2017
卷:173
期:Complete
页码:584-592
全文大小:1004 K
卷排序:173
文摘
The interactions of HSA with individual or combined EGCG and FU were investigated. Site identification experiments showed that both EGCG and FU mainly bind to subdomain IIA. A competition binding model for the ternary system based on complex was proposed. The secondary structure of HSA was altered due to the binding of EGCG and FU. Competitive binding of EGCG and FU to HSA may enhance anticancer efficacy.