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Published on: September 20, 2016
Protein binding characteristics of 2'-benzoyloxycinnamaldehyde
Ren Shan1, Kyoung-Jin Lee, Byoung-Mog Kwon
1College of Pharmacy, Pusan National University, Pusan, Korea.
Abstract:
The protein binding characteristic of 2'-Benzoyloxycinnamaldehyde (BCA) was investigated, which has demonstrated a potent antitumor effect against several human solid tumor cell lines and in human tumor xenograft nude mice. Protein binding of BCA in human serum was 86 +/- 0.91% and the predominant binding protein of BCA was fatty-acid-free human serum albumin (HSA) (81 +/- 0.91%). The binding of BCA to HSA was outlined by one class, and Ka and n of BCA were 1.65 x 10(5) M(- 1) and 0.374, respectively. Displacement studies with fluorescence probes suggested that BCA mainly binds to site I on HSA, and BCA-induced enhancement in site II binding. The limited drug-drug interaction experiments suggested that BCA influences both site I and site II drug-HSA bindings via different mechanisms; a competitive displacement and a probable allosteric conformational change in HSA, respectively.
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