• Journal of Applied Biological Chemistry
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• v.62 no.1
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• pp.101-107
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• 2019

The objectives of this study were to evaluate the anti-aging effects and investigate the effect of simulated gastrointestinal (GI) digestion on the anti-aging properties and intestinal permeation of the potential fish collagen hydrolysates (FCH). Therefore, procollagen synthesis, matrix metalloproteinase-1 (MMP-1) production, and Caco-2 cell permeability were analyzed before and after in vitro digestion for FCHs, low-molecular weight fractions (<1 kDa), and high molecular weight fractions (>1 kDa). After being subjected to GI digestion, the level of MMP-1 inhibition was maintained, although the procollagen production was significantly (>20%) lower with all samples. Also, the digested FCHs and their <1 kDa fraction yielded 9.1 and 13.8% increased peptide transport, respectively, compared to undigested samples. Based on the effective intestinal permeation and high digestive enzyme stability, the <1 kDa fraction of FCHs is a potential bioactive material suitable for anti-aging applications in the food and cosmetics industries.

• Korean Journal of Materials Research
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• v.34 no.4
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• pp.215-222
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• 2024

Because collagen is inherently piezoelectric, research is being actively conducted to utilize it to harvest energy. In this study, a collagen solution was prepared using edible low-molecular-weight peptide collagen powder, and collagen films were fabricated using a dip coating method. The collagen films prepared by dip coating showed a smooth surface without defects such as pinholes or cracks. Dehydrothermal treatment of the collagen films was performed to induce a stable molecular structure through cross-linking. The collagen film subjected to dehydrothermal treatment at 110 ℃ for 24 h showed a thickness reduction rate of 19 %. Analysis of the collagen films showed that the crystallinity of the collagen film improved by about 7.9 % after dehydrothermal treatment. A collagen film-based piezoelectric nanogenerator showed output characteristics of approximately 13.7 V and 1.4 ㎂ in a pressure test of 120 N. The generator showed a maximum power density of about 2.91 mW/m² and an output voltage of about 8~19 V during various human body movements such as finger tapping. The collagen film-based piezoelectric generator showed improved output performance with improved crystallinity and piezoelectricity after dehydrothermal treatment.

• Fisheries and Aquatic Sciences
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• v.14 no.3
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• pp.174-178
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• 2011

This study aimed to determine the degree of hydrolysis and angiotensin-I-converting enzyme (ACE)-inhibitory activity of Giant Jellyfish Nemopilema nomurai (jellyfish) hydrolysates. The degree of hydrolysis using six proteolytic enzymes (Alcalase, Flavozyme, Neutrase, papain, Protamex, and trypsin) ranged from 13.1-36.8% and the inhibitory activities from 20.46-79.58%. Using papain hydrolysate, we newly isolated and characterized ACE-inhibitory peptides with a molecular weight of 3,000-5,000 Da that originated from jellyfish collagen. The purified peptide (FII-b) was predicted to be produced from an alpha-2 fragment of the type IV collagen of jellyfish. The N-terminal sequence of FII-b was Asp-Pro-Gly-Leu-Glu-Gly-Ala-His-Gly- and showed 87% identity to the collagen type IV alpha-2 fragment of Rattus norvegicus and a predicted protein from Nematostella vectensis, indicating that the ACE-inhibitory peptide originated from the collagen hydrolysate and had an $IC_{50}$ value of 3.8 ${\mu}g$/mL. The primary structure of the fragment is now being studied; this peptide represents an interesting new type of ACE inhibitor and will provide knowledge of the potential applications of jellyfish components as therapies for hypertension.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.46 no.3
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• pp.243-252
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• 2020

Using Fervidobacterium islandicum AW-1, polar low molecular weight keratin peptides were produced and confirmed through factors related to the skin elasticity. As a result of confirming the cytotoxicity and collagen synthesis ability according to the concentration of the polar low molecular weight keratin peptide in human fibroblasts, it was confirmed that the cytotoxicity did not appear and the collagen synthesis in human fibroblasts was increased. A mask pack containing a polar low-molecular weight keratin peptide was used, and a test product was used for 4 weeks in 22 healthy women subjects. As a result, it showed statistically significant effects on skin elasticity, skin torsion elasticity, skin color and moisture improvement. Through this test, it was confirmed that the polar low-molecular keratin peptide can be used as a cosmetic ingredient that helps improve skin elasticity.

• The Journal of Korean Medicine Ophthalmology and Otolaryngology and Dermatology
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• v.23 no.3
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• pp.33-41
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• 2010

Background & Objective : This study was performed to find a new anti-aging, anti-wrinkle agent. Ten kinds of hers were evaluated by proliferation, cytotoxicity, collagen synthesis tests in cultured human dermal fibroblast. Methods : MTT assay was carried out to check cell proliferation, cytotoxic effect of each herbal medicine. Collagen synthesis was investigated by the amount of propeptide using procollagen type-Ⅰ C peptide(PIP) ELISA kit(Takara). Results and Conclusions : There are no cytotoxicity in all group herbs by MTT assay. Collagen synthetic ability was greatest in LYCII FRUCTUS(LF) and was excellent in order of Rehmanniae Radix Preparat(RRP) > Nelumbinis Semen(NS) > Asparai Radix(AR) > Schizandrae Frucus(SF).

• Proceedings of the Korean Society of Toxicology Conference
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• 2002.11b
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• pp.161-161
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• 2002

The abnormal accumulation of collagen is progressive and often results in impairment of liver function, i.e. liver cirrhosis. Collagen synthesis requires several posttranslational events. Prolyl 4-hydroxylase is the key enzyme in collagen synthesis that catalyzes the hydroxylation of peptide-bound proline residues to 4-hydroxyroline.(omitted)

• Mass Spectrometry Letters
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• v.12 no.3
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• pp.81-84
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• 2021

Collagen, which accounts for one-third of human protein, is reduced due to human aging, and much attention is focused on making collagen into food to prevent such aging. Gel permeation chromatography with Reflective Index (RI) detection (GPC/RI) was chosen as the most suitable instrument to confirm molecular weight distribution, and we explored the use of this technique for analysis of collagen peptide molecular sizes and distributions. Data reliability was verified by matrix-assisted laser desorption/ionization coupled to time-of-flight (MALDI-TOF) mass spectrometric analysis. The data were considered meaningful for comparative analysis of molecular weight distribution patterns.

• Journal of Integrative Natural Science
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• v.9 no.2
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• pp.86-93
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• 2016

The peptide sequences, GHK(Gly-His-Lys) and KTTKS(Lys-Thr-Thr-Lys-Ser), using a collagen stimulator recently were manipulated at N-terminal as a multifunctional peptide derivative with PEG(polyethyleneglycol) linker connected to gallic acid which presents anti-inflammatory activity. The multifunctional peptide derivatives were obtained in a normal peptide preparation method through SPPS(solid phase peptide synthesis) using Fmoc chemistry and a carboxyl group insertion reaction of PEG-3,4,5-triacetoxy benzoate by using potassium tert-butoxide and ethyl bromoacetate, which was separated by Sephadex DEAE. It gave a good compromise to a cosmetic application for cell cytotoxicity, anti-wrinkle, and anti-inflammation.

• Applied Chemistry for Engineering
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• v.24 no.1
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• pp.62-66
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• 2013

This study was performed to investigate the physicochemical characteristics of glycoprotein extracted from carrot. We manufactured glycoprotein using natural vegetable raw materials carrots, and then analyzed it's physicochemical properties. The results showed that the nutritional composition of carrot glycoprotein (CG) consisted of 2.35% carbohydrate and 94.2% glycoprotein. There were small amounts of hydroxyproline and glycine known as characteristics of collagen peptide in the amino acid of CG, but there were large amount of glutamic acid and aspartic acid involved in the metabolism of glucose and fat. The calories of CG was 342.1 kcal/100 g and the molecular weight appeared less than 594 Da average molecular weight distribution.

• BMB Reports
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• v.40 no.4
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• pp.532-538
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• 2007

Mouse ficolin A is a plasma protein with lectin activity, and plays a role in host defense by binding carbohydrates, especially GlcNAc, on microorganisms. The ficolin A subunit consists of an N-terminal signal peptide, a collagen-like domain, and a C-terminal fibrinogen-like domain. In this study, we show that ficolin A can be synthesized and oligomerized in a cell and secreted into culture medium. We also identify a functionally relevant signal peptide of ficolin A by using MS/MS analysis to determine the N-terminal sequence of secreted ficolin A. When the signal peptide of mouse ficolin A was fused with enhanced green fluorescent protein (EGFP), EGFP was released into HEK 293 cell medium, suggesting that the signal peptide can efficiently direct ficolin A secretion. Moreover, our results suggest that the signal peptide of ficolin A has potential application for the production of useful secretory proteins.