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1.
Nutrients ; 15(11)2023 May 24.
Artigo em Inglês | MEDLINE | ID: mdl-37299410

RESUMO

The mechanism of silver carp scale collagen peptides (SCPs1) on melanogenesis and its mechanism of action were examined in mouse melanoma cells (B16). The cell viability and effects of SCPs1 on intracellular tyrosinase (TYR) activity and melanin, reactive oxygen species (ROS), glutathione (GSH) and cyclic adenosine monophosphate (cAMP) content were examined. The regulatory mechanism of SCPs1 on the cAMP response element-binding protein (CREB) signaling pathway was analyzed. The cell viability of the SCPs1 group was >80% (0.01-1 mg/mL) and the inhibitory rate of SCPs1 on B16 cell melanin increased in a dose-dependent manner. The highest inhibitory rate of SCPs1 on melanin content reaching 80.24%. SCPs1 significantly increased the GSH content and decreased the tyrosinase activity, as well as the content of ROS and cAMP. Western blot analysis showed that SCPs1 significantly inhibited melanocortin-1 receptor (MC1R) expression and CREB phosphorylation in the cAMP-CREB signaling pathway, leading to downregulation of microphthalmia-associated transcription factor (MITF) and the expression of TYR, TYR-related protein-1 (TRP-1) and TRP-2. SCPs1 also inhibited the expression of MC1R, MITF, TYR, TRP-1 and TRP-2 at the transcriptional level. Taken together, SCPs1 inhibited melanin synthesis through the downregulation of the cAMP-CREB signaling pathway. Fish-derived collagen peptides could potentially be applied in skin whitening products.


Assuntos
Melaninas , Melanoma Experimental , Animais , Camundongos , Regulação para Baixo , Monofenol Mono-Oxigenase/metabolismo , Espécies Reativas de Oxigênio/metabolismo , Melanoma Experimental/metabolismo , Linhagem Celular Tumoral , Transdução de Sinais , Peptídeos/farmacologia , Peptídeos/metabolismo , Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/metabolismo
2.
Foods ; 12(10)2023 May 09.
Artigo em Inglês | MEDLINE | ID: mdl-37238751

RESUMO

Swim bladder polypeptides (SBPs) of Acipenser schrencki were analyzed for their antioxidant activity and physicochemical properties. The results showed the optimal enzymatic conditions were alkaline protease with a solid-to-liquid ratio of 1:20, an incubation time of 4 h, a temperature of 55 °C, and an enzyme dosage of 5000 U/g. Three different molecular weight fractions (F1, F2, and F3) were obtained via ultrafiltration. F3 (912.44-2135.82 Da) showed 77.90%, 72.15%, and 66.25% removal of O2•-, DPPH•, and •OH, respectively, at 10 mg/mL, which was significantly higher than the F1 and F2 fractions (p < 0.05). F3 contained proline (6.17%), hydroxyproline (5.28%), and hydrophobic amino acids (51.39%). The UV spectrum of F3 showed maximum absorption at 224 nm. Peptide sequence analysis showed that F3 contained antioxidant peptides (MFGF, GPPGPRGPPGL, and GPGPSGERGPPGPM) and exhibited inhibitory activities on angiotensin-converting enzyme and dipeptidyl peptidase III/IV (FRF, FPFL and LPGLF). F3 was considered a good raw material for obtaining bioactive peptides.

3.
Foods ; 12(7)2023 Apr 06.
Artigo em Inglês | MEDLINE | ID: mdl-37048373

RESUMO

This study involves the preparation of scale collagen peptides (SCPs) with whitening activity from silver carp (Hypophthalmichthys molitrix) and their characterization and peptide sequence identification. In this article, scanning electron microscopy (SEM) was used to observe structure changes of sliver carp scales; enzymatic hydrolysis was optimized through protease screening and response surface optimization. The ultrafiltration was used to separate SCPs and the whitening activity was comprehensively evaluated using radical scavenging rate and tyrosinase-inhibiting activity, among others. An optimal component was characterized and identified using various modern spectral analysis techniques. The results showed that the surface of silver carp scales after decalcification was smooth and clear. The pepsin had the highest peptide yield and tyrosinase-inhibiting activity (90.01% and 82.25%, respectively). The optimal enzymatic hydrolysis conditions were an enzyme dosage of 16.1%, a solid-liquid ratio of 1:15.6 and a time of 4.9 h. The proportions of hydrophobic and basic amino acids in the peptide composition were 32.15% and 13.12%, respectively. Compared with SCPs2, SCPs1 (6096.68-9513.70 Da) showed better ·OH scavenging ability, tyrosinase-inhibiting activity and moisture absorption. SCPs1 was a macromolecular fragment of type I collagen with a triple helix structure, containing three peptide sequences with the potential for tyrosinase activity inhibition (AGPPGADGQTGQRGE, SGPAGIAGPAGPRGPAGPNGPPGKD and KRGSTGEQGSTGPLGMRGPRGAA). These results show that SCPs1 is a collagen peptide product with whitening potential.

4.
Front Nutr ; 8: 812443, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-35059429

RESUMO

To explore the physicochemical properties and biological functions of silver carp scale peptide (SCSP), its molecular-weight fractions SCSP-I, II, and III obtained by nanofiltration were assessed for their solubility, emulsibility, free radical scavenging ability, effect on the proliferation of mouse B16 cells. The results showed that the solubility of each fraction of SCSP was higher than 90%, SCSP-II and III were higher than 95%. The antioxidant powers on ⦁OH, O 2 - ⦁ and Fe3+ were ranked as SCSP-III > SCSP-II > SCSP-I > SCSP. All fractions of SCSP had no toxic or side effects in mouse B16 melanoma cells experiments in vitro. At a concentration of 0.01 mg/mL, the tyrosinase activity of B16 cells in the SCSP-II fraction was significantly lower than that of the α-arbutin (P < 0.05), at 65.37%. The molecular weight distribution of SCSP was 399-1404 Dalton and 13 peptide sequences were detected. Among them, SCSP-II contained many hydrophobic amino acids, and SCSP-III stood out for combining arginine with hydrophobic amino acids. This may be the reason why the low molecular-weight SCSPs show the strong antioxidant activity and strong tyrosinase inhibition. The work provides a data base for the development of SCSP and increases the possibility of its application.

5.
J Sci Food Agric ; 100(12): 4612-4617, 2020 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-32418235

RESUMO

BACKGROUND: Irradiation can cause lipid oxidation of fish. This study aimed to examine the effect of radiation (method, dose and dose rate) on the acid value (AV), peroxide value (PV), thiobarbituric acid reactive substances (TBARS) content and fatty acid profile of fresh and freeze-dried largemouth bass flesh. RESULTS: AV, PV and TBARS presented a dose-dependent increase in fish meat for both cobalt-60 (60 Co) and electron beam (EB) irradiation. With a 6 kGy dose of radiation, all measured indices in the 60 Co group were significantly higher than those in the EB group (P < 0.05 or P < 0.01). With a 3 kGy dose of radiation, AV, PV and TBARS in the 200 Gy min-1 dose rate group were significantly lower than those in the 2 and 80 Gy min-1 groups (P < 0.05). After 60 Co irradiation, AV, PV and TBARS in most fresh samples were significantly higher than those in freeze-dried samples (P < 0.01). And 60 Co irradiation decreased the unsaturated fatty acid (UFA) content in fresh samples and increased the UFA content in freeze-dried samples. Our study indicated that 60 Co irradiation, particularly at a low dose rate, accelerated lipid oxidation in fish meat. A large amount of muscle moisture enhances the amount of UFA loss in fish meat during 60 Co irradiation. CONCLUSIONS: A low dose (3 kGy) of EB irradiation, a high dose rate (200 Gy min-1 ) of 60 Co irradiation or freeze-drying treatment can alleviate the lipid oxidation of largemouth bass meat. © 2020 Society of Chemical Industry.


Assuntos
Radioisótopos de Cobalto/química , Irradiação de Alimentos/métodos , Lipídeos/química , Carne/efeitos da radiação , Animais , Bass , Ácidos Graxos Insaturados/química , Carne/análise , Oxirredução
6.
Biomed Rep ; 2(3): 388-391, 2014 May.
Artigo em Inglês | MEDLINE | ID: mdl-24748980

RESUMO

This study was conducted to evaluate the sedative effects of Arachis hypogaea L. stem and leaf extract (AHSLE) and determine its effect pathways through γ-aminobutyric acid (GABA)-gated channels on male Sprague-Dawley rats treated with pentobarbital. AHSLE was obtained from 98°C water (3 h, extracted twice). AHSLE and flumazenil (a GABA type A receptor antagonist) were administered to the rats orally, whereas pentobarbital sodium and muscimol (a GABA type A receptor agonist) were administered intraperitoneally (i.p.). The results demonstrated that AHSLE decreased sleep latency and increased sleep time in pentobarbital-treated rats (50 mg/kg, i.p.). The coadministration of AHSLE and muscimol (0.05 mg/kg) significantly increased sleep time and reduced sleep latency in pentobarbital-treated rats and these actions were significantly antagonized by flumazenil at a dose of 3.5 mg/kg. These results indicated that AHSLE improved the sleep behavior in pentobarbital-treated rats, possibly through GABA-gated channel-related mechanisms.

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