Previous Article in Journal
Fractions of Concern: Challenges and Strategies for the Safety Assessment of Biological Matter in Cosmetics
Previous Article in Special Issue
Anti-Inflammatory Activity of Calendula officinalis L. Flower Extract
Open AccessArticle

Potent Tyrosinase Inhibitory Activity of Curcuminoid Analogues and Inhibition Kinetics Studies

1
Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Burapha University, Bangsaen, Chonburi 20131, Thailand
2
International College of Dentistry, Walailak University, Nakhon Si Thammarat 80161, Thailand
3
Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Ramkhamhaeng University, Bangkapi, Bangkok 10240, Thailand
4
Université Côte d’Azur, CNRS, ICN, 28 Avenue Valrose, CEDEX 2, 06108 Nice, France
*
Authors to whom correspondence should be addressed.
Academic Editor: Enzo Berardesca
Cosmetics 2021, 8(2), 35; https://doi.org/10.3390/cosmetics8020035
Received: 9 April 2021 / Revised: 27 April 2021 / Accepted: 28 April 2021 / Published: 4 May 2021
(This article belongs to the Special Issue Feature Papers in Cosmetics in 2021)
Natural tyrosinase inhibitors from herbal plants are promising therapeutic agents for skincare and cosmetic products. Natural curcuminoids exhibit weak antityrosinase properties. The structural modification of curcumin, the major curcuminoid from Curcuma longa, gave 14 analogues. The tyrosinase inhibitory activity of the natural curcuminoids and the modified analogues on both L-tyrosine and DOPA substrates were evaluated. The inhibition kinetics were also undertaken. For analogues with potent activity on the L-tyrosine substrate, the isoxazole analogue 12 and two reduced analogues, hexahydrocurcumin (16) and the α,β-unsaturated analogue 17, showed IC50 values of 8.3, 14.6 and 9.4 µM, and were 20.9-, 11.9- and 18.4-fold more active, respectively, than kojic acid, the reference compound. For the analogues with potent antityrosinase on DOPA substrate, the dimethylated analogue 5 exhibited the strongest antityrosinase activity against the DOPA substrate, with the IC50 value of 8.0 µM, which was 16.6-fold more active than kojic acid. The inhibition kinetics revealed that curcuminoid 5 could bind with both free enzyme and with the enzyme–substrate complex. It acted as a competitive–uncompetitive mixed-II type inhibitor. Curcuminoid 17 could bind with both free enzyme and the enzyme–substrate complex. The results indicated that 17 acted as a competitive–uncompetitive mixed-I type inhibitor, while curcuminoid 12 was a noncompetitive inhibitor which bound with both free enzymes and the enzyme–substrate complex. These potent analogues might serve as new potential tyrosinase inhibitors for the prevention and treatment of skin pigmentation disorders. View Full-Text
Keywords: curcuminoid analogues; antityrosinase activity; inhibition kinetics; skin pigmentation disorders curcuminoid analogues; antityrosinase activity; inhibition kinetics; skin pigmentation disorders
Show Figures

Figure 1

MDPI and ACS Style

Athipornchai, A.; Niyomtham, N.; Pabuprapap, W.; Ajavakom, V.; Duca, M.; Azoulay, S.; Suksamrarn, A. Potent Tyrosinase Inhibitory Activity of Curcuminoid Analogues and Inhibition Kinetics Studies. Cosmetics 2021, 8, 35. https://doi.org/10.3390/cosmetics8020035

AMA Style

Athipornchai A, Niyomtham N, Pabuprapap W, Ajavakom V, Duca M, Azoulay S, Suksamrarn A. Potent Tyrosinase Inhibitory Activity of Curcuminoid Analogues and Inhibition Kinetics Studies. Cosmetics. 2021; 8(2):35. https://doi.org/10.3390/cosmetics8020035

Chicago/Turabian Style

Athipornchai, Anan; Niyomtham, Nattisa; Pabuprapap, Wachirachai; Ajavakom, Vachiraporn; Duca, Maria; Azoulay, Stéphane; Suksamrarn, Apichart. 2021. "Potent Tyrosinase Inhibitory Activity of Curcuminoid Analogues and Inhibition Kinetics Studies" Cosmetics 8, no. 2: 35. https://doi.org/10.3390/cosmetics8020035

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop