Skin hyperpigmentation resulting from excessive tyrosinase expression has long been a problem for beauty lovers, which has not yet been completely solved. Although researchers are working on finding effective tyrosinase inhibitors, most of them are restricted, due to cell mutation and cytotoxicity. Therefore, functional foods are developing rapidly for their good biocompatibility. Food-derived peptides have been proven to display excellent anti-tyrosinase activity, and the mechanisms involved mainly include inhibition of oxidation, occupation of tyrosinase’s bioactive site and regulation of related gene expression. For anti-oxidation, peptides can interrupt the oxidative reactions catalyzed by tyrosinase or activate an enzyme system, including SOD, CAT, and GSH-Px to scavenge free radicals that stimulate tyrosinase. In addition, researchers predict that peptides probably occupy the site of the substrate by chelating with copper ions or combining with surrounding amino acid residues, ultimately inhibiting the catalytic activity of tyrosinase. More importantly, peptides reduce the tyrosinase expression content, primarily through the cAMP/PKA/CREB pathway, with PI3K/AKT/GSK3β, MEK/ERK/MITF and p38 MAPK/CREB/MITF as side pathways. The objective of this overview is to recap three main mechanisms for peptides to inhibit tyrosinase and the emerging bioinformatic technologies used in developing new inhibitors.

The objective of this research was to investigate the antioxidant activity of Gracilarialemaneiformis polysaccharide degradation and its underlying mechanism involved in the Nrf-2/Keap-1 signaling pathway in HepG2 cells with oxidative stress induced by H₂O₂. The result of the scavenging ability of free radicals showed that GLP-HV (polysaccharide degraded by H₂O₂–vitamin C (Vc)) performed a better scavenging ability than GLP (G.lemaneiformis polysaccharide). Moreover, the scavenging ability of polysaccharide to these free radicals from strong to weak was as follows: superoxide radical, ferric ion, ABTS⁺, and DPPH radical, and their IC₅₀ values were 3.56 ± 0.0028, 4.97 ± 0.18, 9.62 ± 0.35, and 23.85 ± 1.78 mg/mL, respectively. Furthermore, GLP-HV obviously relieved oxidative stress in HepG2 cells, which strengthened the activity of T-AOC, CAT, GSH-PX, and SOD, and diminished the intensity of MDA, intracellular ROS, and calcium ion based on the Nrf-2/Keap-1 signaling pathway. The PCR result revealed that polysaccharide upregulated the expression of the genes Nrf-2, HO-1, NQO-1, and ZO-1 and downregulated Keap-1. The correlation between chemical properties and antioxidant mechanism of GLP-HV was evaluated via a heat map. The results illustrated that reducing sugar and active groups presented a positive correlation, and molecular weight and viscosity exhibited a negative relation with antioxidant activity.

• Gracilaria lemaneiformis, rich in polysaccharide, is a kind of economic red algae. • The extraction, purification, structure and bioactivities of GLP were provided. • The mechanisms of bioactivities of GLP were described. • The urgent problems to be solved are raised in this paper.

The objective of the present study was to investigate the xanthine oxidase (XO) inhibitory effects of peptides purified and identified from round scad (Decapterus maruadsi) hydrolysates (RSHs). In this study, RSHs were obtained by using three proteases (neutrase, protamex and alcalase). Among them, the RSHs of 6-h hydrolysis by neutrase displayed the strongest XO inhibitory activity and had an abundance of small peptides (<500 Da). Four novel peptides were purified by immobilized metal affinity chromatography and identified by nano-high-performance liquid chromatography mass/mass spectrometry. Their amino acid sequences were KGFP (447.53 Da), FPSV (448.51 Da), FPFP (506.59 Da) and WPDGR (629.66 Da), respectively. Then the peptides were synthesized to evaluate their XO inhibitory activity. The results indicated that the peptides of both FPSV (5 mM) and FPFP (5 mM) exhibited higher XO inhibitory activity (22.61 ± 1.81% and 20.09 ± 2.41% respectively). Fluorescence spectra assay demonstrated that the fluorescence quenching mechanism of XO by these inhibitors (FPSV and FPFP) was a static quenching procedure. The study of inhibition kinetics suggested that the inhibition of both FPSV and FPFP was reversible, and the type of their inhibition was a mixed one. Molecular docking revealed the importance of π-π stacking between Phe residue (contained in peptides) and Phe⁹¹⁴ (contained in the XO) in the XO inhibitory activity of the peptides.