tyrosinase inhibitors
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Author(s):  
Cigdem Dokuzparmak ◽  
Fulya Oz Tuncay ◽  
Serap Basoglu Ozdemir ◽  
Busra Kurnaz ◽  
Ilke Demir ◽  
...  

2021 ◽  
Vol 37 (1) ◽  
pp. 421-430
Author(s):  
Katarzyna Jakimiuk ◽  
Suat Sari ◽  
Robert Milewski ◽  
Claudiu T. Supuran ◽  
Didem Şöhretoğlu ◽  
...  

Biophysica ◽  
2021 ◽  
Vol 1 (4) ◽  
pp. 458-473
Author(s):  
Maria Evgenia Politi ◽  
Kostas Bethanis ◽  
Trias Thireou ◽  
Elias Christoforides

Numerous natural products and designed molecules have been evaluated as tyrosinase inhibitors that impede enzymes’ oxidation activity. In the present study, new potent natural inhibitors were retrieved from the ZINC database by the similarity-screening of 37 previously reported tyrosinase inhibitors. The screening resulted in 42 candidate inhibitory molecules that were categorized into five groups. Molecular-docking analysis for these compounds, as well as for three others known for their inhibition activity (caffeic acid, naringenin, and gallic acid), was carried out against the tyrosinase structure from Agaricus bisporus (AbTYR). The top-scoring compounds were used for further comparative analysis with their corresponding naturally occurring glycosides. The results suggested that the glycosylated inhibitors could interact better with the enzyme than their aglycon forms. In order to further examine the role of the sugar side group of potent tyrosinase inhibitors, the dynamic behavior of two such pairs of glycosidic/aglycol forms (naringin–naringenin and icariin–icaritin) in their complexes with the enzyme were studied by means of 20-ns MD simulations. The increased number of intermolecular hydrogen bonds and their augmented lifetime between AbTYR and the glycosidic analogues showed that the naringin and icariin molecules form more stable complexes than naringenin and icaritin with tyrosinase, and thus are more potent inhibitors.


2021 ◽  
pp. 132283
Author(s):  
Nima Sepehri ◽  
Mehdi Khoshneviszadeh ◽  
Sara Moghadam Farid ◽  
Seyedeh Sara Moayedi ◽  
Mohammad Sadegh Asgari ◽  
...  

Catalysts ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1430
Author(s):  
Klaudia Karkeszová ◽  
Mária Mastihubová ◽  
Vladimír Mastihuba

Kojic acid is a fungal metabolite and one of the strongest tyrosinase inhibitors. Its esters are used as lipid-compatible skin whitening components in cosmetic formulations. In this study, lipase PS, lipase AK, Lipolyve AN and pig pancreatic lipase catalyzed the acetylation of kojic acid under selective formation of the same product, kojic 7-acetate. However, the enzymes differed in their regioselectivity when catalyzing the alcoholysis of kojic acid diacetate. While lipase PS and lipase AK produced mixtures of both monoacetate regioisomers (7-acetate and 5-acetate of kojic acid), the pancreatic lipase almost exclusively produced 5-acetate. The enzyme displayed the same regioselectivity in the palmitoylation of kojic acid and in the alcoholysis of kojic acid dipalmitate. Simple reaction engineering with PPL as a catalyst thus provides the complementary monoesters of kojic acid. Kojic 7-acetate, 5-acetate, 7-palmitate and 5-palmitate were prepared with yields after purification of 57.3%, 38.2%, 31.7% and 31.4%, respectively.


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