TITLE

Interaction Between Amino Acid Derivatives of Aspirin and Human Serum Albumin

AUTHOR(S)
CHANG, H. H.; M. MI, M.; LI, X.; GAO, W. C.; WEI, W. L.
PUB. DATE
November 2015
SOURCE
Asian Journal of Chemistry;2015, Vol. 27 Issue 12, p4392
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Aspirin, with simple structure and good effects, is one of the most popular antipyretic and anti-inflammatory drugs. Tested more than a century, aspirin was found enough to treat cancer and cardiovascular disease. However, the side effects of aspirin should not be ignored. In order to overcome these side effects, its mechanism of action and drug-modification were pushed to a hot spot. Three amino acid derivatives of aspirin were synthesised and the interaction with human serum albumin were studied via fluorescence spectroscopy. The main binding force between P1, P2 and human serum albumin was mainly van der Waals forces, the interaction of human serum albumin with P3 was mainly electrostatic attraction. Synchronous fluorescence spectroscopy indicated that aspirin and its derivatives have changed the chemical environment of the tryptophan residues, inducing polarity of hydrophobic cavity and stretch of the peptide chain, thus making the protein conformation changed. Amino acid derivatives of aspirin can decrease the fluorescence intensity of human serum albumin, which result from the changing of the chemical environment caused by aspirin and its derivatives.
ACCESSION #
109393671

 

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