A spectroscopic study on the interaction between the anticancer drug erlotinib and human serum albumin

作者：Ye Zuo wu; Ying Yin; Yang Xiu li; Zheng Zao qian; Shi Jia na; Sun Yun feng; Huang Ping^*

来源：Journal of Inclusion Phenomena and Macrocyclic Chemistry, 2014, 78(1-4): 405-413.

DOI：10.1007/s10847-013-0311-4

• Serum albumin
• Erlotinib
• Fluorescence
• Circular dichroism
• UV-Vis
• FTIR

The interaction between erlotinib and human serum albumin (HSA) in simulated physiological conditions was investigated by spectroscopic methods. The results revealed that erlotinib caused the fluorescence quenching of HSA through a static quenching procedure. The binding constants at 293, 298, 303 and 308 K were obtained as 2.53 x 10(5), 8.13 x 10(4), 3.59 x 10(4) and 1.93 x 10(4) M-1, respectively. There may be one binding site of erlotinib on HSA at 298 K. The thermodynamic parameters indicated that the interaction between erlotinib and HSA was driven mainly by hydrogen bonding or van der Waals forces. Synchronous fluorescence spectra, UV-Vis spectra, circular dichroism and Fourier Transform infrared spectroscopy results showed erlotinib binding slightly changed the conformation of HSA with secondary structural content changes. Forster resonance energy transfer study revealed high possibility of energy transfer with erlotinib-Trp-214 distance of 3.48 nm. The results of the present study may provide valuable information for studying the distribution, toxicological and pharmacological mechanisms of erlotinib in vivo.

• 出版日期2014-4
• 单位浙江省中医药研究院