Protein Binding Characteristics of 2′-Benzoyloxycinnamaldehyde

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.

Key Words:

• Cinnamaldehyde
• Protein binding
• Displacement