Evaluation of TILI-2 as an Anti-Tyrosinase, Anti-Oxidative Agent and Its Role in Preventing Melanogenesis Using a Proteomics Approach

• Published in: Molecules (Basel, Switzerland) Vol. 27; no. 10; p. 3228
• Main Authors: Joompang, Anupong, Anwised, Preeyanan, Klaynongsruang, Sompong, Roytrakul, Sittiruk, Taemaitree, Lapatrada, Jangpromma, Nisachon
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 18.05.2022; MDPI
• Subjects: Animals; antioxidant; Antioxidants; Chromatography, Liquid; Competition; Cytotoxicity; Enzymes; Fibroblasts; Hyperpigmentation; Macrophages; mass spectrometry; Melanin; Melanins; Mice; Monophenol Monooxygenase; monophenolase activity; Online data bases; peptide; Peptides; Proteins; Proteomics; Signal transduction; Tandem Mass Spectrometry; Tyrosinase; tyrosinase inhibitor; tyrosinase inhibitor; mass spectrometry; antioxidant; peptide; monophenolase activity
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules27103228

There is a desire to develop new molecules that can combat hyperpigmentation. To this end, the N-terminal cysteine-containing heptapeptide TILI-2 has shown promising preliminary results. In this work, the mechanism by which it works was evaluated using a series of biochemical assays focusing on known biochemical pathways, followed by LC-MS/MS proteomics to discover pathways that have not been considered before. We demonstrate that TILI-2 is a competitive inhibitor of tyrosinase's monophenolase activity and it could potentially scavenge ABTS and DPPH radicals. It has a very low cytotoxicity up to 1400 µM against human fibroblast NFDH cells and macrophage-like RAW 264.7 cells. Our proteomics study revealed that another putative mechanism by which TILI-2 may reduce melanin production involves the disruption of the TGF-β signaling pathway in mouse B16F1 cells. This result suggests that TILI-2 has potential scope to be used as a depigmenting agent.