Studies on the interaction between triazole derivative and human serum albumin by spectroscopy and molecular modeling
Yue Yuan-yua
Abstract
Yue Yuan-yua
Abstract
The interaction between 1-benzyl- 4-phenyl- 1H- 1,2,3-triazole( BPT) and human serum albumin( HSA) was investigated by spectroscopic methods and the molecular modeling technique. Synchronous fluorescence and three-dimensional fluorescence spectroscopy suggested perturbation in the structure of HSA in the presence of BPT and an increase in the hydrophobicity around the fluorophore in HSA. Molecular modeling indicated that the binding of BPT to HSA was most likely located within a hydrophobic cavity of subdomain IIA.The results of molecular modeling revealed that there were hydrogen bonds between Arg222 and BPT.
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The interaction between 1-benzyl- 4-phenyl- 1H- 1,2,3-triazole( BPT) and human serum albumin( HSA) was investigated by spectroscopic methods and the molecular modeling technique. Synchronous fluorescence and three-dimensional fluorescence spectroscopy suggested perturbation in the structure of HSA in the presence of BPT and an increase in the hydrophobicity around the fluorophore in HSA. Molecular modeling indicated that the binding of BPT to HSA was most likely located within a hydrophobic cavity of subdomain IIA.The results of molecular modeling revealed that there were hydrogen bonds between Arg222 and BPT.
Key concepts: Chemistry, Human serum albumin, Molecular model, Fluorophore, Hydrogen bond, Fluorescence spectroscopy, Fluorescence, Hydrophobic effect