Paving the way towards effective plant-based inhibitors of hyaluronidase and tyrosinase: a critical review on a structure-activity relationship

Abstract

Human has used plants to treat many civilisation diseases for thousands of years. Examples include reserpine (hypertension therapy), digoxin (myocardial diseases), vinblastine and vincristine (cancers), and opioids (palliative treatment). Plants are a rich source of natural metabolites with multiple biological activities, and the use of modern approaches and tools allowed finally for more effective bioprospecting. The new phytochemicals are hyaluronidase (Hyal) inhibitors, which could serve as anti-cancer drugs, male contraceptives, and an antidote against venoms. In turn, tyrosinase inhibitors can be used in cosmetics/pharmaceuticals as whitening agents and to treat skin pigmentation disorders. However, the activity of these inhibitors is stricte dependent on their structure and the presence of the chemical groups, e.g. carbonyl or hydroxyl. This review aims to provide comprehensive and in-depth evidence related to the anti-tyrosinase and anti-Hyal activity of phytochemicals as well as confirming their efficiency and future perspectives.

Keywords: Hyaluronidase; polyphenols; structure–activity relationship; tyrosinase plant-based inhibitors.

Graphical abstract

Figure 1.

Classification of hyaluronidases (HMWHA: long-chain hyaluronic acid; LMWHA: short-chain hyaluronic acid).

Figure 2.

Chemical groups of flavonoids involved in the inhibition of hyaluronidase.

Figure 3.

Effect of alkyl chain length in phenolic acids on activity against hyaluronidase.

Figure 4.

Potential groups engaged in an interaction oligomers phenolic acids-hyaluronidase.

Figure 5.

Potential groups engaged in an interaction fukiic acid derivative-hyaluronidase.

Figure 6.

Chemical classification of tannins.

Figure 7.

Structure of benzylisoquinoline alkaloids and apomorphine alkaloids.

Figure 8.

Chemical groups of L-ascorbic acid involved in the inhibition of hyaluronidase.

Figure 9.

Chemical structures of saponins. A – triterpene saponins, B – steroid saponins, C – steroid alkaloids, and D – isoprene.

Figure 10.

Chemical groups of triterpenic acids involved in the inhibition of hyaluronidase.

Figure 11.

3-O-β-D-glucuronopyranoside group.

Figure 12.

A – reaction hydroxylation of monophenols to o-diphenols; reaction B – oxidation of o-diphenols to o-quinones.

Figure 13.

Mechanism of the tyrosinase action as monophenolase and diphenolase.

Figure 14.

The pathway of melanin synthesis.

Figure 15.

a) Potential groups engaged in an interaction hydroxybenzoic acid-tyrosinase and b) Potential groups engaged in an interaction hydroxycinnamic acid-tyrosinase.

Figure 16.

Potential groups engaged in an interaction flavonoid-tyrosinase.

Figure 17.

Structure relationship between flavanol (a) and kojic acid (b) and mode of copper chelation by 3-hydroxy-4-keto group in flavanol (c), and kojic acid (d).

Figure 18.

Chemical classification of lignans.

Figure 19.

Chemical structure of cis- and trans-isomer of stilbenes.

Figure 20.

Potential groups engaged in an interaction stilbene-tyrosinase.

Figure 21.

a) A basic structure of chalcones (1,3-diphenyl-2-propen-1-one); b) The difference in structure between stilbenes and chalcones.

Figure 22.

a) Similarity in the structure of L-tyrosine and 4-hydroxychalcones; b) Similarity in structure of L-DOPA and flavonol.

Figure 23.

Potential groups engaged in an interaction chalcone-tyrosinase.

Figure 24.

Structure of Phenlpropanoid Sucrose Esters – PSEs (R: phenylpropanoid residues).

Figure 25.

Structure of α-piron (a); benzo-α-piron (b).

Figure 26.

Potential groups engaged in an interaction coumarin-tyrosinase.