• Journal of Applied Biological Chemistry
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• 제62권1호
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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.

• 한국재료학회지
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• 제34권4호
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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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• 제14권3호
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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.

• 대한화장품학회지
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• 제46권3호
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• pp.243-252
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• 2020

본 연구에서는 Fervidobacterium islandicum AW-1를 이용하여 극성 저분자 케라틴 펩타이드를 생산하고, 피부 탄력과 관련한 인자를 확인하여, 화장품 원료로서 극성 저분자 케라틴 펩타이드의 가능성을 확인하였다. 인체섬유아세포에 극성 저분자 케라틴 펩타이드를 농도에 따라 세포독성 및 콜라겐 합성능을 확인한 결과, 세포 독성은 나타나지 않았고, 인체섬유아세포 내 콜라겐 합성을 증가시키는 것을 확인하였다. 극성 저분자 케라틴 펩타이드를 함유한 마스크팩을 만들어, 22 명의 건강한 성인 피험자를 대상으로 4 주 동안 시험제품을 사용한 결과, 피부 탄력 및 피부 비틀림 탄력 개선, 수분량 증가, 피부색 개선에서 통계적으로 유의한 효과를 나타냈다. 이를 통해 극성 저분자 케라틴 펩타이드는 피부 탄력 개선에 도움을 주는 화장품 원료로 사용할 수 있음을 확인하였다.

• 한방안이비인후피부과학회지
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• 제23권3호
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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).

• 한국독성학회:학술대회논문집
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• 한국독성학회 2002년도 Molecular and Cellular Response to Toxic Substances
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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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• 제12권3호
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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.

• 통합자연과학논문집
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• 제9권2호
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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.

• 공업화학
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• 제24권1호
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• pp.62-66
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• 2013

본 연구는 당근에서 추출한 당근당단백질(carrot glycoprotein, 이하 CG라 명함)의 물리화학적인 특성을 조사하기위하여 수행되었다. 천연 식물성 원료인 당근에서 CG를 제조하여 물리화학적인 특성을 분석하였다. 영양성분 조성을 분석한 결과 CG는 당단백질로서 2.35%의 탄수화물과 94.2%의 단백질로 구성되어있는 것으로 나타났다. 아미노산 조성분석 결과 CG는 콜라겐 펩타이드의 특징인 hydroxyproline과 glycine은 소량 검출되었으며, 포도당과 지방 대사에 관여하는 glutamicacid와 asparticacid가 높게 검출되었다. 또한 열량 분석결과 100 g의 CG는 342.1 kcal의 열량을 지니고 있는 것으로 나타났다. CG의 분자량 분석 결과에서는 594 Da 이하의 평균분자량 분포를 나타내는 특성을 가지고 있는 것을 알 수 있었다.

• BMB Reports
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• 제40권4호
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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.