Protein binding characteristics of 2'-benzoyloxycinnamaldehyde = 벤조일옥시시남알데하드와 단백질과의 상호작용

Cited 2 time in scopus
Metadata Downloads
Protein binding characteristics of 2'-benzoyloxycinnamaldehyde = 벤조일옥시시남알데하드와 단백질과의 상호작용
R Shan; K J Lee; Byoung-Mog Kwon; C H Lee
Bibliographic Citation
Drug Development and Industrial Pharmacy, vol. 31, no. 6, pp. 545-549
Publication Year
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 × 105 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.
cinnamaldehydedisplacementprotein binding
T&F (Taylor & Francis)
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.

Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.