Evaluation of collagenase, elastase and tyrosinase inhibitory activities of Cotinus coggygria Scop. through in vitro and in silico approaches

Şenol Deniz F. S. , Salmas R. E. , Emerce E., Çankaya İ. İ. , Yusufoglu H. S. , Erdoğan Orhan İ.

SOUTH AFRICAN JOURNAL OF BOTANY, vol.132, pp.277-288, 2020 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 132
  • Publication Date: 2020
  • Doi Number: 10.1016/j.sajb.2020.05.017
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Geobase, Veterinary Science Database
  • Page Numbers: pp.277-288
  • Keywords: Cotinus coggygria, Collagenase, Elastase, Molecular docking, PASS screening, Tyrosinase, MUTAGENIC ACTIVITY, QUERCETIN, FLAVONOIDS, EXTRACT, CONSTITUENTS, ANTIOXIDANT
  • Gazi University Affiliated: Yes


Cotinus coggygria Scop. (Anacardiaceae, syn: Rhus cotinus L.) is known as "boyaci sumagi, sari boya, duman agaci" in Turkish and "smoke tree" in English. It is commonly grown in Southern Europe and Anatolia. The leaves have been used due to its antiseptic, hemostatic, antipyretic, and wound healing effects as a 5% infusion in traditional medicine. It has also been reported to be used against skin disorders in Russia. Based on this information, the ethanol extracts prepared from the pedicels and leaves of C. coggygria were investigated for their elastase, collagenase, and tyrosinase inhibitory effects, which are enzymes related to anti-aging, using ELISA microtiter assays. Based on our results, the ethanol extracts prepared from the leaves and pedicels of C. coggygria had low elastase (28.16% +/- 2.91 and 25.76% +/- 1.71, respectively), moderate collagenase (47.78% +/- 4.90 and 46.51% +/- 3.15, respectively), and tyrosinase (57.94% +/- 0.67 and 46.20% +/- 0.92, respectively) inhibition at final concentration (666mg/mL). The ethanol extract prepared from the pedicels of C. coggygria was subjected to bioactivity-guided fractionation, which led to isolation of methyl gallate, astragalin, isoquercetin, and hyperoside from the active fractions. In addition to the enzyme assays, in order to understand the inhibition mechanisms of the compounds inside the ligand-binding domains, the interactions were simulated and the key amino acids contributing to the hydrogen bonds and non-polar interactions with the ligands were reported. (c) 2020 SAAB. Published by Elsevier B.V. All rights reserved.