| Issue |
BIO Web Conf.
Volume 8, 2017
2016 International Conference on Medicine Sciences and Bioengineering (ICMSB2016)
|
|
|---|---|---|
| Article Number | 01021 | |
| Number of page(s) | 6 | |
| Section | Session I: Medicine | |
| DOI | https://doi.org/10.1051/bioconf/20170801021 | |
| Published online | 11 January 2017 | |
Study on interaction between salicylaldehyde l-serine schiff base and human serum albumin by fluorescence spectroscopy
School of Pharmacy, Henan University of Chinese Medicine, Zhengzhou 450046, China
a Corresponding author: yanghuaixia886@163.com
The interaction of salicylaldehyde L-serine Schiff base (L) with human serum albumin (HSA) was examined by fluorescence emission spectra at the excitation wavelength 290 nm. Through fluorescence quenching experiments, it was confirmed that the combination of L with HSA was static quenching process. Thermodynamic parameters, such as ΔG, ΔH and ΔS, were calculated at different temperatures, showing that van der Waals force or hydrogen bond interaction were mostly responsible for the binding of L to HSA. The experiments results showed that the microenvironment and the conformation of HSA changed during the binding reaction.
This study was supported by HenanProvince basic and frontier technology researchprojects (152300410214), Program for the key scientific research project of colleges and universitiesin Henan Province (16A350002), and Science & Technology Innovation Talents in Henan College of Chinese Medicine (2014XCXRC04).
© The Authors, published by EDP Sciences, 2017
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