Effects of Isorhamnetin on Tyrosinase: Inhibition Kinetics and Computational Simulation

2012 ◽  
Vol 76 (6) ◽  
pp. 1091-1097 ◽  
Author(s):  
Yue-Xiu SI ◽  
Zhi-Jiang WANG ◽  
Daeui PARK ◽  
Hyoung Oh JEONG ◽  
Sen YE ◽  
...  
2013 ◽  
Vol 48 (1) ◽  
pp. 152-161 ◽  
Author(s):  
Yue-Xiu Si ◽  
Sunyoung Ji ◽  
Wei Wang ◽  
Nai-Yun Fang ◽  
Qing-Xin Jin ◽  
...  

2012 ◽  
Vol 50 (1) ◽  
pp. 257-262 ◽  
Author(s):  
Yue-Xiu Si ◽  
Zhi-Jiang Wang ◽  
Daeui Park ◽  
Hae Young Chung ◽  
Su-Fang Wang ◽  
...  

2011 ◽  
Vol 29 (3) ◽  
pp. 463-470 ◽  
Author(s):  
Shang-Jun Yin ◽  
Yue-Xiu Si ◽  
Zhi-Jiang Wang ◽  
Su-Fang Wang ◽  
Sangho Oh ◽  
...  

Author(s):  
Zhi-Jiang Wang ◽  
Sunyoung Ji ◽  
Yue-Xiu Si ◽  
Jun-Mo Yang ◽  
Guo-Ying Qian ◽  
...  

2012 ◽  
Vol 2012 ◽  
pp. 1-10 ◽  
Author(s):  
Hong-Jian Liu ◽  
Sunyoung Ji ◽  
Yong-Qiang Fan ◽  
Li Yan ◽  
Jun-Mo Yang ◽  
...  

Tyrosinase is a ubiquitous enzyme with diverse physiologic roles related to pigment production. Tyrosinase inhibition has been well studied for cosmetic, medicinal, and agricultural purposes. We simulated the docking of tyrosinase and D-(−)-arabinose and found a binding energy of −4.5 kcal/mol for theup-formof D-(−)-arabinose and −4.4 kcal/mol for thedown-form of D-(−)-arabinose. The results of molecular dynamics simulation suggested that D-(−)-arabinose interacts mostly with HIS85, HIS259, and HIS263, which are believed to be in the active site. Our kinetic study showed that D-(−)-arabinose is a reversible, mixed-type inhibitor of tyrosinase (α-value =6.11±0.98, Ki=0.21±0.19 M). Measurements of intrinsic fluorescence showed that D-(−)-arabinose induced obvious tertiary changes to tyrosinase (binding constant K=1.58±0.02 M−1, binding number n=1.49±0.06). This strategy of predicting tyrosinase inhibition based on specific interactions of aldehyde and hydroxyl groups with the enzyme may prove useful for screening potential tyrosinase inhibitors.


2013 ◽  
Vol 29 (1) ◽  
pp. 92-99 ◽  
Author(s):  
Wei Sun ◽  
Michael Wendt ◽  
Gerhard Klebe ◽  
Klaus-Heinrich Röhm

2011 ◽  
Vol 48 (4) ◽  
pp. 700-704 ◽  
Author(s):  
Yue-Xiu Si ◽  
Shang-Jun Yin ◽  
Daeui Park ◽  
Hae Young Chung ◽  
Li Yan ◽  
...  

2010 ◽  
Vol 9 (1) ◽  
pp. 158-168
Author(s):  
Lanny Hartanti ◽  
Henry Kurnia Setiawan

Cinnamic acid is one of known tyrosinase inhibitors. This study investigated the inhibition of tyrosinase activity of some cinnamic acid derivatives, i.e. 4-buthoxy-cinnamic acid, 4-n-butylcinnamic acid and 4-phenylcinnamic acid. Each inhibitor used in this research had the same type of inhibition towards enzymatic activity, i.e. mixed type inhibition of competitive and non competitive type. The potential sequence of tyrosinase inhibition based on the ratio of its IC50 compared to cinnamic acid, from the lowest to the highest were 4-buthoxycinnamic acid, 4-phenylcinnamic acid and 4-n-butylcinnamic acid. Based on the obtained results of this research, it was disclosed that n-butyl substituent on para position did not increase the inhibition effect of cinnamic acid towards tyrosinase enzymatic reaction. But in the other hand, buthoxy and phenyl substituent on para position could increase the inhibition effect of cinnamic acid towards tyrosinase enzymatic reaction because buthoxy substituent increased the similarity of its structure with the substrate of enzymatic reaction while phenyl susbtituent blocked the substrate-enzyme reaction.   Keywords: tyrosinase; L-DOPA; inhibition kinetics; IC50, cinnamic acid


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