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Title 

Protein binding characteristics of 2'-benzoyloxycinnamaldehyde

 

벤조일옥시시남알데하드와 단백질과의 상호작용

Authors 

R ShanK J LeeByoung-Mog KwonC H Lee

Publisher 

Informa Healthcare

Issue Date 

2005

Citation 

Drug Development and Industrial Pharmacy, vol. 31, no. 6, pp. 545-549

Keywords 

cinnamaldehydedisplacementprotein binding2' benzoyloxycinnamaldehydebinding competitionbinding sitedrug protein binding

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 × 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.

ISSN 

0363-9045

Link 

http://dx.doi.org/10.1080/03639040500215651

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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