AI Article Synopsis
- Nature-derived tyrosinase inhibitors are important for various industries, and a study focused on three monophenolase inhibitor peptides (MIPs) and three diphenolase inhibitor peptides (DIPs) to evaluate their effectiveness against tyrosinase and other properties.
- DIP1 emerged as the strongest inhibitor, showcasing a strong binding ability with tyrosinase due to specific aromatic amino acid interactions, and its copper-chelating capabilities contributed to its effectiveness.
- Additionally, DIP1 exhibited the best sun protection factor (SPF) and notable antioxidant activities, indicating its potential for use in pharmaceuticals and cosmetics.
Article Abstract
Nature-derived tyrosinase inhibitors are of great industrial interest. Three monophenolase inhibitor peptides (MIPs) and three diphenolase inhibitor peptides (DIPs) from a previous study were investigated for their in vitro tyrosinase inhibitory effects, mode of inhibition, copper-chelating activity, sun protection factor (SPF) and antioxidant activities. DIP1 was found to be the most potent tyrosinase inhibitor (IC = 3.04 ± 0.39 mM), which could be due to the binding interactions between its aromatic amino acid residues (Y2 and D7) with tyrosinase hotspots (H85, V248, H258, H263, F264, R268, V283 and E322) and its ability to chelate copper ion within the substrate-binding pocket. The conjugated planar rings of tyrosine and tryptophan may interact with histidine within the active site to provide stability upon enzyme-peptide binding. This postulation was later confirmed as the Lineweaver-Burk analysis had identified DIP1 as a competitive inhibitor and DIP1 also showed 36.27 ± 1.17% of copper chelating activity. In addition, DIP1 provided the highest SPF value (11.9 ± 0.04) as well as ferric reducing antioxidant power (FRAP) (5.09 ± 0.13 mM FeSO), 2,2'-azinobis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) (11.34 ± 0.90%) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) (29.14 ± 1.36%) free radical scavenging activities compared to other peptides. These results demonstrated that DIP1 could be a multifunctional anti-tyrosinase agent with pharmaceutical and cosmeceutical applications.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8004729 | PMC |
| http://dx.doi.org/10.3390/foods10030675 | DOI Listing |
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