Citation: Chen Dandan, Zou Jiajia, Du Chuanrong, Luo Xuan, Lin Cuiwu. Syntheses of L-Tyrosine Derivatives and Their Interaction with Human Serum Albumin[J]. Chemistry, ;2016, 79(7): 623-629,644. shu

Syntheses of L-Tyrosine Derivatives and Their Interaction with Human Serum Albumin

  • Corresponding author: Lin Cuiwu, 
  • Received Date: 29 November 2015
    Available Online: 3 March 2016

    Fund Project:

  • Two L-tyrosine derivatives, (E)-3-(4'-hydroxyphenyl)-2-[3"-(2'''-methoxyphenyl)acrylamido]propanoic acid (I) and (E)-3-(4'-hydroxyphenyl)-2-[3"-(3'''-methoxyphenyl)acrylamido]propanoic acid (II), were synthesized from o-methoxycinnamic acid and m-methoxycinnamic acid respectively. Their structures were characterized by ESI-MS, 1H NMR and 13C NMR. The mechanism of the interaction between derivatives and human serum albumin (HSA) was researched by the fluorescence emission spectra, synchronous fluorescence spectra, UV-Vis spectra and molecular docking. The results indicated that the quenching mechanism of derivatives and HSA was static. The process was accompanied with the non-radiative energy transfer. Hydrophobic interaction was the predominant intermolecular force in the combination of derivatives and HSA. The process was spontaneous. Molecular docking showed that the hydrophobic cavity of the subdomain IIA (site I) was the location of the binding site of derivative I/II and HSA. Hydrophobic interaction contributed to their combination, which was consistent with the experimental results.
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