Binding <Emphasis Type="Italic">Citrus</Emphasis> flavanones to human serum albumin: effect of structure on affinity |
| |
Authors: | Hui Cao Longsheng Chen Jianbo Xiao |
| |
Institution: | (1) School of Chemistry and Chemical Engineering, Nantong University, Nantong, 226007, People’s Republic of China;(2) Application Research Laboratory, Anhui Academy of Science & Technology, Hefei, Anhui, People’s Republic of China;(3) College of Life & Environment Science, Shanghai Normal University, 100 Guilin Rd, Shanghai, 200234, People’s Republic of China; |
| |
Abstract: | Much of the bioactivities of Citrus flavanones significantly appear to impact blood and microvascular endothelial cells. It is essential to investigate the interaction
between Citrus flavanones and serum albumin to verify the effect of flavanone structures on the distribution and transportation in blood.
The interactions between flavonoids and proteins have attracted great interest among researchers. The work in here mainly
concerns about the binding interaction between Citrus flavanones and human serum albumin (HSA) in vitro. The methoxylation of tangeretin improved the affinity for HSA by 100 times.
The 2,3-double bond in conjugation with a 4-oxo group plays an important role for the affinity for HSA. The affinity of apigenin
for HSA is about 10,000-times higher than that of naringenin. It was found that the hydroxylation on position 3′ of flavonol
significantly improves the binding affinity for HSA. The affinity of quercetin (3′, 4′) for HSA is about 100-times higher
than that of kaempferol (4′). The hydroxylation on position 3′ of flavone slightly improves the binding affinity for HSA.
The affinity of luteolin for HSA is about 1.38-times higher than that of apigenin. The values of log10(Ka) are proportional to the number of binding sites (n), which confirms the method used here is suitable to study the interaction between Citrus flavanones and HSA. |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|