Structural identification and combination mechanism of iron (II)-chelating Atlantic salmon (Salmo salar L.) skin active peptides.

In order to utilize salmon skin for high value, and investigate the structural identification and combination mechanism of iron (II)-chelating peptides systemically, Atlantic salmon (Salmo salar L.) skin, a by-product of Atlantic salmon processing, was treated by two-step enzymatic hydrolysis to obtain salmon skin active peptides (SSAP). Then they reacted with iron (II) to obtain iron (II)-chelating salmon skin active peptides (SSAP-Fe) with a high iron (II) chelating ability of 98.84%. The results of Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD) spectroscopy, 8-anilino-1-naphthalenesulfonic acid ammonium salt hydrate (ANS) combined fluorescence measurement, isothermal titration calorimetry (ITC) and full wavelength ultraviolet (UV) scanning showed that the structural characteristics of SSAP changed before and after chelating iron (II). Reverse phase high performance liquid chromatography (RP-HPLC) and mass spectrometry were used to identify and quantify the peptides in SSAP-Fe. Four peptide sequences (STEGGG, GIIKYGDDFMH, PGQPGIGYDGPAGPPGPPGPPGAP and QNQRESWTTCRSQSSLPDG) were identified. The content of PGQPGIGYDGPAGPPGPPGPPGAP was the highest, at 25.17 µg/mg. The pharmacokinetic and pharmacodynamic properties of these four peptides were also investigated, and the results indicated that they have satisfactory predicted ADMET properties. Molecular docking technology was used to analyze the binding sites between iron (II) and SSAP, and it was found that PGQPGIGYDGPAGPPGPPGPPGAP had the lowest predicted binding energy with iron (II) and the most stable predicted binding energy with iron (II). This results showed that the stability of SSAP-Fe were closely related to the number of covalent bonds and the types of amino acids. This study revealed the structure and combination mechanism of SSAP-Fe, and indicated that SSAP-Fe prepared by chelation may be used as a Fe supplement that can be applied in functional foods or ingredients.

Effects of topical application of different molecular weight marine fish skin collagen oligopeptides on UVB-induced photoaging rat skin.

OBJECTIVE: The objective of this work was to develop a peptide production process of the exact molecular weight propitious to topical application for cosmetics and to investigate the effects of enzymolysis-derived peptide on UVB-induced photoaging rat skin. METHODS: The chum salmon fish skins were hydrolyzed by alkaline protease and neutral protease and spray-dried at different conditions, and three kinds of molecular weight peptide (MFSOP) were obtained. A total of 66 ICR rats (female, 20 ± 1 g) were randomly divided into eleven groups, including the normal, model, and experimental groups. The three kinds of MFSOP were dissolved at different dosages (5‰, 2.5%, and 5%) and then applied on the ICR hairless back skins prior to exposing UVB irradiation of 3000mJ/cm2 to them 4 h later. After 8 weeks, the rats were killed and the hair-shaved skins were tested for skin moisture, hyaluronic acid, hydroxyproline, antioxidant activity, and RNA expression. RESULTS: Three kinds of MFSOP were obtained, with the average molecular weights of 495.16, 1194.00, and 2032.46 Dalton, respectively. The MFSOPs, especially the MFSOP of average molecular weight of 1194.00 Dalton, played an important role in the recovery of the UVB-injured skin tissue in lock in moisture, in antioxidant activity and in promotion in collagen and elastin protein to some extent. CONCLUSION: MFSOPs, especially MFSOP of average molecular weight of 1194.00 Dalton, derived from enzymolysis are potential materials to apply in cosmetics for the UVB9-induced anti-photoaging activity (lock in moisture, antioxidant activity, and promotion in collagen and elastin protein).

Inhibitory effect of hesperetin on α-glucosidase: Molecular dynamics simulation integrating inhibition kinetics.

The α-glucosidase inhibitor is of interest to researchers due to its association with type-2 diabetes treatment. Hesperetin is a flavonoid with natural antioxidant properties. This paper presents an evaluation on the effects of hesperetin on α-glucosidase via inhibitory kinetics using a Molecular Dynamics (MD) simulation integration method. Due to the antioxidant properties of hesperetin, it reversibly inhibits α-glucosidase in a slope-parabolic mixed-type manner (IC50=0.38±0.05mM; Kslope=0.23±0.01mM), accompanied by tertiary structural changes. Based on computational MD and docking simulations, two hesperetin rings interact with several residues near the active site on the α-glucosidase, such as Lys155, Asn241, Glu304, Pro309, Phe311 and Arg312. This study provides insight into the inhibition of α-glucosidase by binding hesperetin onto active site residues and accompanying structural changes. Hesperetin presents as a potential agent for treating α-glucosidase-associated type-2 diabetes based on its α-glucosidase-inhibiting effect and its potential as a natural antioxidant.