We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
欧前胡素对酪氨酸酶的抑制作用及机制.
- Authors
张国文; 石文丽; 朱 苗
- Abstract
The inhibitory effect of imperatorin on tyrosinase and its mechanism were studied by UV, fluorescence and circular dichroism spectroscopy combined with molecular simulation technology. The results showed that imperatorin was a reversible mixed-type inhibitor with a half inhibitory concentration (IC50) of 7.90×10-5 mol·L-1. The endogenous fluorescence of tyrosinase is quenched in a morphological manner, and the two have a binding site. The binding constant at 25 °C is 2.90 × 10³ L.mol-1, and the hydrophobic effect Force is the main force driving the combination of the two. Simultaneous fluorescence and circular dichroism analysis show that imperatorin has a strong effect on tyrosine and tryptophan residues in tyrosinase. The surrounding microenvironment has little effect, but causes the secondary structure of tyrosinase to become loose. Molecular simulations show that imperatorin occupies the activity of tyrosinase. It interacts with amino acid residues such as His244, Val283, Val286, His263, etc., preventing the binding of the substrate to the active center of the enzyme, thereby reducing the activity of the enzyme. Low tyrosinase catalytic activity.
- Subjects
MOLECULAR spectroscopy; NANOTECHNOLOGY; AMINO acid residues; CIRCULAR dichroism; HYDROPHOBIC interactions; PHENOL oxidase
- Publication
Journal of Nanchang University (Natural Science), 2021, Vol 45, Issue 5, p463
- ISSN
1006-0464
- Publication type
Article