College of Chemistry and Materials Science, Analysis and Testing Center, Jiangsu Key Laboratory of Biofunctional Materials, Nanjing Normal University, Nanjing 210046, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2012 Oct;96:461-7. doi: 10.1016/j.saa.2012.05.059. Epub 2012 Jun 2.
In this article, the interaction mechanism of prodigiosin (PG) with bovine hemoglobin (BHb) is studied in detail using various spectroscopic technologies. UV-vis absorption and fluorescence spectra demonstrate the interaction process. The Stern-Volmer plot and the time-resolved fluorescence study suggest the quenching mechanism of fluorescence of BHb by PG is a static quenching procedure, and the hydrophobic interactions play a major role in binding of PG to BHb. Furthermore, synchronous fluorescence studies, Fourier transform infrared (FTIR) and circular dichroism (CD) spectra reveal that the conformation of BHb is changed after conjugation with PG.
本文采用多种光谱技术详细研究了灵菌红素（PG）与牛血红蛋白（BHb）的相互作用机制。紫外-可见吸收光谱和荧光光谱证明了相互作用的过程。Stern-Volmer 图和时间分辨荧光研究表明，PG 对 BHb 荧光的猝灭机制是一种静态猝灭过程，疏水相互作用在 PG 与 BHb 的结合中起主要作用。此外，同步荧光研究、傅里叶变换红外（FTIR）和圆二色（CD）光谱表明，PG 与 BHb 结合后其构象发生变化。
