Spectroscopic Studies on Interactions Between Human Serum Albumin and Nonivamide
  
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KeyWord:surface-enhanced Raman spectroscopy(SERS)  fluorescence spectrum  nonivamide  interaction  human serum albumin(HSA)
  
AuthorInstitution
ZHOU Jia-yu,ZHOU Guang-ming,CHEN Rong,LUO Dan Key Laboratory of Luminescence and Real-time Analysis of the Ministry of Education,School of Chemistry and Chemical Engineering,Southwest University,Chongqing ,China
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Abstract:
      Under simulated physiological conditions,the adsorption mode of nonivamide(OC) on the surface of AuNPs was determined with AuNPs as the Raman substrate.Surface-enhanced Raman spectroscopy(SERS) revealed that the phenolic group of OC combined with human serum albumin(HSA).The influence of HSA on the adsorption mode of OC after recognition was analyzed,and the thermodynamic parameters for the interaction between OC and HSA were calculated.The main binding forces were hydrogen bonds,hydrophobic interaction force and Vander Waals force.and the interaction was strong.The results of fluorescence spectroscopy indicated that OC slightly affected the secondary structure of HSA,and increased the hydrophobicity of the microenvironment around the tryptophan residue.The information could be used not only as a reference for study on the mechanism of interaction between drugs and blood plasma or serum albumin,but also as a guidance to understand the metabolism of drugs in human body.
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