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

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Abstract

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 × 105, 8.13 × 104, 3.59 × 104 and 1.93 × 104 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. Förster 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.

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Acknowledgments

This work was supported by Natural Science Foundation of Zhejiang Province of China (No. Y2110933).

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Authors and Affiliations

  1. Department of Pharmacy, Tongde Hospital of Zhejiang Province, 234 Gucui Road, Hangzhou, 310012, China

    Zuo-wu Ye, Yin Ying, Xiu-li Yang, Zao-qian Zheng, Jia-na Shi, Yun-feng Sun & Ping Huang

  2. Zhejiang Academy of Traditional Chinese Medicine, 132 Tianmushan Road, Hangzhou, 310007, China

    Ping Huang

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  1. Zuo-wu Ye
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Correspondence to Ping Huang.

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Ye, Zw., Ying, Y., Yang, Xl. et al. A spectroscopic study on the interaction between the anticancer drug erlotinib and human serum albumin. J Incl Phenom Macrocycl Chem 78, 405–413 (2014). https://doi.org/10.1007/s10847-013-0311-4

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