Review on marine collagen peptides induce cancer cell apoptosis,necrosis,and autophagy by reducing oxidized free radicals

Marine collagen peptides(MCPs)are natural products prepared by hydrolyzing marine collagen protein through a variety of chemical methods or enzymes.MCPs have a range of structures and biological activities and are widely present in marine species.MCPs also have a small molecular weight,are easily modified,and absorbed by the body.These properties have attracted great interest from researchers studying antioxidant,anti-tumor,and anti-aging activities.MCPs of specific molecular weights have significant anti-tumor activity and no toxic side effects.Thus,MCPs have the potential use as anti-cancer adjuvant drugs.Free radicals produced by oxidation are closely related to human aging,cancer,arteriosclerosis,and other diseases,but their relationship with cancer is not well known.In this review,we focus on the antioxidant properties of MCPs in the treatment of cancer,highlighting their antioxidant molecular structure and potential for clinical practice.

Recent progress in preventive effect of collagen peptides on photoaging skin and action mechanism

Ultraviolet(UV)-induced photoaging skin has become an urgent issue.The functional foods and cosmetics aiming to improve skin photoaging are developing rapidly,and the demand is gradually increasing year by year.Collagen peptides have been proven to display diverse physiological activities,such as excellent moisture retention activity,hygroscopicity,tyrosinase inhibitory activity and antioxidant activity,which indicates that they have great potential in amelioration of UV-induced photoaging.The main objective of this article is to recap the main mechanisms to improve photoaging skin by collagen peptides and their physiological activities in photo-protection.Furthermore,the extraction and structural characteristics of collagen peptides are overviewed.More importantly,some clinical trials on the beneficial effect on skin of collagen peptides are also discussed.In addition,prospects and challenges of collagen peptides are emphatically elucidated in this review.This article implies that collagen peptides have great potential as an effective ingredient in food and cosmetics industry with a wide application prospect.

Calcium-chelating peptides from rabbit bone collagen:characterization,identification and mechanism elucidation

This study aimed to characterize and identify calcium-chelating peptides from rabbit bone collagen and explore the underlying chelating mechanism.Collagen peptides and calcium were extracted from rabbit bone by instant ejection steam explosion(ICSE)combined with enzymatic hydrolysis,followed by chelation reaction to prepare rabbit bone peptide-calcium chelate(RBCP-Ca).The chelating sites were further analyzed by liquid chromatography-tandem mass(LC-MS/MS)spectrometry while the chelating mechanism and binding modes were investigated.The structural characterization revealed that RBCP successfully chelated with calcium ions.Furthermore,LC-MS/MS analysis indicated that the binding sites included both acidic amino acids(Asp and Glu)and basic amino acids(Lys and Arg),Interestingly,three binding modes,namely Inter-Linking,Loop-Linking and Mono-Linking were for the first time found,while Inter-Linking mode accounted for the highest proportion(75.1%),suggesting that chelation of calcium ions frequently occurred between two peptides.Overall,this study provides a theoretical basis for the elucidation of chelation mechanism of calcium-chelating peptides.

Collagen peptide provides Streptomyces coelicolor CGMCC 4.7172 with abundant precursors for enhancing undecylprodigiosin production

Effective and ecofriendly converting biomass to chemicals is important for sustainable engineering based on the foreseeable shortage of fossil resources.Undecylprodigiosin(UP)is a promising antibiotic,but the direct feeding of pure precursor amino acids makes it costly for large-scale production.Here,collagen peptide(CP),a renewable animal-derived biomass contains abundant precursor amino acids of UP.CP can act as carbon and nitrogen source for the growth of Streptomyces coelicolor CGMCC 4.7172.The plant biomasses including soybean meal,wheat bran,and malt extract were unsuitable for UP prodution.However,365.40µg/L UP was detected after 24 h in the media containing CP,and its highest concentration reached 1198.01µg/L.UP was also detected in the media containing meat hydrolysates of domestic animals,but its initial production time was delayed,and final concentration was lower than that in the medium containing CP only.Compared the fermentation performances of CP and other proteins,CP has a special superiority for UP production.These results revealed that UP biosynthesis may be dependent on amino acid availability of substrates and CP is beneficial for UP production because of its specific amino acid composition.

Interaction mechanism of collagen peptides with four phenolic compounds in the ethanol-water solution

This study demonstrated the interaction mechanism of collagen peptides(CPs)with 4-ethylphenol(4-EP),phenol,guaiacol,and 4-ethylguaiacol(4-EG)in the ethanol-water solution.The ultraviolet visible spectroscopy,zeta potential tests and hydrogen nuclear magnetic spectroscopy manifested that CPs interacted with the phenolic compounds.Meanwhile,Isothermal titration calorimetry determination indicated that the CPs was hydrogen bonded with 4-EP in 52%(v/v)ethanol-water solution,while the hydrophobic forces played a major role in the interaction of CPs with guaiacol and 4-EG,respectively.Moreover,hydrogen and hydrophobic bonds were involved in the interaction between CPs and phenol.Finally,Head Space-solid Phase Microextraction Gas Chromatography Mass Spectrometry analysis indicated that the content of phenolic compounds in model solution efficiently decreased with the presence of CPs.In the real liquor,it was found that the content of volatile compounds(including phenolic compounds)was obviously decreased after CPs added.

Antioxidant and anti-HepG2 cell activities of a novel bioactive peptide from cowhide collagen in vitro

In the present study,the antioxidant and anti-human liver cancer(HepG2)cells effects of bioactive peptides from cowhide collagen(BPCC)were evaluated.BPCC exhibited significant scavenging effect on l,1-diphenyl-2-picrylhydrazyl(DPPH)radicals((60.09±3.51)%),2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)(ABTS)radicals((77.40±3.10)%)and hydroxyl radicals((56.00±2.30)%)as well as strong reducing power(0.320士0.025).Meanwhile,BPCC effectively protected biomacromolecules including proteins,lipids and DNA from oxidative damage induced by Cu^(2+)H_(2)O_(2)and 2,2'-azobis(2-methylpropionamidine)dihydrochloride(AAPH).Moreover,BPCC significantly inhibited cell viability of HepG2 cells in a dose-dependent manner with an estimated IC_(50)of 7.61 mg/mL.The results of 4',6-diamidino-2-phenylindole(DAPI)and acridine:orange/ethidium bromide(AO/EB)staining demonstrated the apoptotic morphological changes and cell mediated death in BPCC treated HepG2 cells.In addition,BPCC induced decrease of mitochondrial membrane potential(MMP)in HepG2 cells.Therefore,the present finding proved that BPCC encompasses significant antioxidant activity and anticancer property on HepG2 cells and can be used as alternative food antioxidants for cancer prevention benefits.

Chicken collagen hydrolysates differentially mediate anti-inflammatory activity and type I collagen synthesis on human dermal fibroblasts

Collagen is a major extracellular matrix protein.Given the potential anti-inflammatory and antioxidant profiles of these bioactive compounds,there has been increasing interest in using collagen derived peptides and peptide-rich collagen hydrolysates for skin health,due to their immunomodulatory,antioxidant and proliferative effects on dermal fibroblasts.However,all hydrolysates are not equally effective in exerting the beneficial effects;hence,further research is needed to determine the factors that improve the therapeutic applicability of such preparations.We used different enzymatic conditions to generate a number of different collagen hydrolysates with distinct peptide profiles.We found that the use of two rather than one enzyme for hydrolysis generates a greater abundance of low molecular weight peptides with consequent improvement in bioactive properties.Testing these hydrolysates on human dermal fibroblasts showed distinct actions on inflammatory changes,oxidative stress,type I collagen synthesis and cellular proliferation.Our findings suggest that different enzymatic conditions affect the peptide profile of hydrolysates and differentially regulate their biological activities and potential protective responses on dermal fibroblasts.

Beauty from within: A Review of the Science behind Yuliv^TMCollagen Drink: An Anti-Aging Nutraceutical

The use of nutraceuticals to improve skin properties and decelerate skin aging has been gaining attention among dermatologists, over the last years. In this article, we are presenting the theoretical scientific support for YulivTM Collagen Drink, a liquid supplement containing bovine type I collagen peptides, ascorbic acid and Camellia sinensis (green tea) extract and its benefits on the skin. The available literature shows that the ingredients contained in the supplement have the potential to improve of skin hydration, dermis collagen density, and decrease the fragmentation of the dermal collagen network—and therefore reduce wrinkles and sagging and improving elasticity. Additionally, other health benefits could also be observed, such as protection against oxidative stress, contribution to the normal function of the immune system and reducing tiredness and fatigue, and reduction of skin inflammation, improvement of elasticity and prevention of oxidation. For those benefits to be visible, it is likely that continuous use of at least 4 weeks is needed.

Effect of hydrophilic or hydrophobic interactions on the self-assembly behavior and micro-morphology of a collagen mimetic peptide

Peptide self-assembles with bionic properties have been widely utilized for bioactive drugs and biomedical materials.Collagen mimetic peptide(CMP)gains more attention due to its unique advantages in biosecurity and function.Unfortunately,the self-assembly mechanism of CMP,particularly the effect of intermolecular forces on its self-assembly behavior and morphology,is still unrecognized.Herein,the hydrophilic glycidol(GCD)and hydrophobic Y-glycidyl ether oxypropyl trimethoxysilane(GLH)were grafted onto the side chains of CMP through the ring-opening reaction(GCD/CMP,GLH/CMP).Subsequently,the effects of hydrophilic and hydrophobic interactions on the self-assembly behavior and morphology of CMP were further studied.The results substantiated that the GCD/CMP and GLH/CMP self-assembly followed“nucleation-growth”mechanism,and the supererogatory hydrophilic and hydrophobic groups prolonged the nucleation and growth time of CMP self-assembly.Noted that the hydrophilic interaction had stronger driving effects than hydrophobic interaction on the self-assembly of CMP.The GCD/CMP and GLH/CMP self-assembles exhibited fibrous 3D network and microsphere morphology,respectively.Furthermore,the GLH/CMP self-assembles had better resistance to degradation.Consequently,the microtopography and degradation properties of CMP self-assembles could be controlled by the hydrophilic and hydrophobic interactions between CMP,which would further provide a way for subsequent purposeful design of biomedical materials.