• Journal of Applied Biological Chemistry
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• v.59 no.3
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• pp.239-242
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• 2016

A novel Nicotinoyl fused peptide, Nicotinoyl-LVH, was synthesized by solid phase peptide synthesis method, purified, and tested in cultured skin cells. Nicotinoyl-LVH enhanced the expression level of collagen mRNA and its fragments in fibroblasts. These data show that this novel Nicotinoyl peptide is a promising biomaterial in the anti-aging functional cosmetic market.

• BMB Reports
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• v.48 no.9
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• pp.501-506
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• 2015

Based on the potential beneficial effects of growth hormone releasing peptide (GHRP)-6 on muscle functions, a newly synthesized GHRP-6-biotin conjugate was tested on cultured myoblast cells. Increased expression of myogenic marker proteins was observed in GHRP-6-biotin conjugate-treated cells. Additionally, increased expression levels of insulin-like growth factor-1 and collagen type I were observed. Furthermore, GHRP-6-biotin conjugate-treated cells showed increased metabolic activity, as indicated by increased concentrations of energy metabolites, such as ATP and lactate, and increased enzymatic activity of lactate dehydrogenase and creatine kinase. Finally, binding protein analysis suggested few candidate proteins, including desmin, actin, and zinc finger protein 691 as potential targets for GHRP6-biotin conjugate action. These results suggest that the newly synthesized GHRP-6-biotin conjugate has myogenic stimulating activity through, at least in part, by stimulating collagen type I synthesis and several key proteins. Practical applications of the GHRP-6-biotin conjugate could include improving muscle condition. [BMB Reports 2015; 48(9): 501-506]

• BMB Reports
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• v.42 no.11
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• pp.743-746
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• 2009

L-ascorbic acid (Vitamin C) and peptide are both useful compounds for collagen biosynthesis in cosmeceuticals (cosmetic and pharmaceutical fields). The instability of these compounds, however, limit their application in these industries. In this report, we describe the development of a novel compound, Stabilized Ascorbyl Pentapeptide (SAP), which physically is much more stable than L-ascorbic acid in water. The inhibitory effects of this SAP compound on tyrosinase and melanin synthesis is comparable to that of L-ascorbic acid. Importantly, the SAP compound displays no cytotoxicity at a high concentration (5 mM). The ability of SAP to promote collagen biosynthesis is greater than that of L-ascorbic acid or the KTTKS peptide alone. Considering the in vitro stability and functional effects, our data strongly suggest that the SAP compound is a good candidate not only as a cosmetic ingredient, but also as a wound healing agent.

• Journal of Korean Biological Nursing Science
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• v.3 no.2
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• pp.91-103
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• 2001

The bone is composed of the bone matrix of collagen and hydroxyapatite, the mixture of calcium and phosphours. The bone tissue is considered to the special connective tissue that possesses extracellular matrix made by collagen fiber deposited with mineral complex. In order to maintain bone mass measured by the sum of bone matrix and hydroxyapatite, bone resorption by osteoclast during lifetime and bone remodeling to form bone by osteoblast in its resorption region repeat continuously. The osteoblast has a mesodermic fetal origin like fibroblast for the formation of form tissues. Two cells express identical genes and synthesize the identical collagen type I as the major component of the formation of bone matrix and skin. Therefore, it is considered that the decrease of skinfold thickness and the decrease of bone mass related to the age, the change of two tissues composed of collagen type I is caused by the same genetic mechanism. The decrease of bone mass is caused by the change of the amount and structure of bone matrix by several factors and the amount of minerals deposited on bone matrix. Especially, in case of female, the deficiency of estrogen by menopause makes these changes rapidly increased. The decrease of bone mass and skinfold thickness is due to the decrease of the amount of collagen and its structural change the common component of bone tissue and skin tissue. Therefore, the relationship of the amount of cross-linked peptide N-telopeptide, collagen metabolite which excretes as urine. Based upon the proved results about the significant relationship of bone mass, the amount of bone collagen, the amount of skin collagen and skinfold thickness, the bone mass may be expected through a facile determination of skinfold thickness.

• Tissue Engineering and Regenerative Medicine
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• v.15 no.6
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• pp.711-719
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• 2018

BACKGROUND: Collagen organization within tissues has a critical role in wound regeneration. Collagen fibril diameter, arrangements and maturity between connective tissue growth factor (CTGF) small interfering RNA (siRNA) and mismatch scrambled siRNA-treated wound were compared to evaluate the efficacy of CTGF siRNA as a future implement for scar preventive medicine. METHODS: Nanocomplexes of CTGF small interfering RNA (CTGF siRNA) with cell penetrating peptides (KALA and $MPG^{{\Delta}NLS}$) were formulated and their effects on CTGF downregulation, collagen fibril diameter and arrangement were investigated. Various ratios of CTGF siRNA and peptide complexes were prepared and down-regulation were evaluated by immunoblot analysis. Control and CTGF siRNA modified cells-populated collagen lattices were prepared and rates of contraction measured. Collagen organization in rabbit ear 8 mm biopsy punch wound at 1 day to 8 wks post injury time were investigated by transmission electron microscopy and histology was investigated with Olympus System and TS-Auto software. CONCLUSION: CTGF expression was down-regulated to 40% of control by CTGF siRNA/KALA (1:24) complexes (p<0.01) and collagen lattice contraction was inhibited. However, down-regulated of CTGF by CTGF $siRNA/MPG^{{\Delta}NLS}$ complexes was not statistically significant. CTGF KALA-treated wound appeared with well formed-basket weave pattern of collagen fibrils with mean diameter of $128{\pm}22nm$ (n = 821). Mismatch siRNA/KALA-treated wound showed a high frequency of parallel small diameter fibrils (mean $90{\pm}20nm$, n = 563). CONCLUSION: Controlling over-expression of CTGF by peptide-mediated siRNA delivery could improve the collagen orientation and tissue remodeling in full thickness rabbit ear wound.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.47 no.2
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• pp.147-153
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• 2021

Collagen hydrolysate (CH) is known to prevent skin aging by stimulating skin dermal fibroblasts to promote synthesis of extracellular matrix such as collagen and elastin. Recently, among the various factors that cause skin aging, advanced glycation end products (AGEs) have received particular attention. However, the effect of CH on AGE accumulation has not been studied. Since CH could affect AGE accumulation by promoting production of skin structural proteins, clinical trial was performed using low molecule collagen peptide (LMCP), which were CH containing 25% tripeptide and 4% Gly-Pro-Hyp. Skin autofluorescence (SAF) values were measured using an AGE reader to evaluate accumulation of AGE in skin. As a result of applying 0.5% and 1.0% LMCP solutions to the subject's forearm for 8 weeks, the SAF value at the test site significantly decreased compared to the control site. Additionally, in vitro test was performed using CCD-986sk to evaluate the promotion of collagen synthesis in skin fibroblasts by LMCP. As a result, 800 ㎍/mL of LMCP significantly increased synthesis of human pro-collagen Iα1 (COL1A1) in CCD-986sk. Through this study, we have confirmed that tropical LMCP applications can promote collagen synthesis to help anti-glycation effects, suggesting that LMCP has potential as an anti-aging cosmetic material.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.41 no.3
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• pp.229-235
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• 2015

Skin aging is the phenomena finally expressed on the skin surface and related to the changes in the microstructure of the skin texture. Which is resulted in wrinkle formation and uneven tone of skin and so on. In this study, the synergy effect of Cedrol and a collagen-derived peptide in type III collagen synthesis was evaluated by in vitro test. The physiological skin state of 22 female volunteers was measured after using the cosmetics for 4 weeks. Results showed that Cedrol and a collagen-derived peptide had the excellent synergy effect in type III collagen synthesis. The cosmetics improved skin microrelief, star configurations, skin gloss, skin tone, hydration and elasticity except skin lightening. In conclusion, this study proved that Cedrol and collagen-derived peptide had the synergy effect of type III collagen synthesis in the cell level and cosmetics with those was improved skin aging in human volunteer test.

• Applied Chemistry for Engineering
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• v.24 no.1
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• pp.18-23
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• 2013

In this research, the collagen peptide powder from flatfish skin (FSCP) was prepared and compared with commercial collagen peptide powder from tilapia scale (TSCP) in the aspect of physiochemical property. The physical property and nutritional components of FSCP appeared almost similarly to those of TSCP, and also in calorie. No differences in calorie between FSCP and TSCP. Amino acid contents of FSCP for example, aspartic acid, serine, histidine, tyrosine and methionine were higher than those of TSCP. In contrast, the hydroxyproline, proline, alanine contents in FSCP were lower than those in TSCP. Especially, the content of essential amino acid of FSCP, which was 22.74%, was higher than that of TSCP evaluated as 13.64%. In the distribution of molecular weight, FSCP was 1000 Da, which showed a comparatively low distribution compared with TSCP, and in emulsion property and stability both FSCP and TSCP showed an excellent trend.

• Journal of the Korea Convergence Society
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• v.11 no.5
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• pp.61-72
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• 2020

An anti-aging peptide was prepared from fish collagen hydrolysate (FCH) by ultrafiltration (MWCO; 1 kDa) and reversed-phased high performance liquid chromatography (RP-HPLC). Its anti-aging properties were evaluated based on the procollagen-synthesizing and MMP-1-inhibiting activities in Hs68 cells. A potent anti-aging peptide (fraction I-I) increased collagen synthesis by 46% and also inhibited MMP-1 secretion by 77%, compared with unpurified FCH. The amino acid sequence of fraction I-I was identified to be Gly-Arg-Arg-Gly-Asn-Lys (GRRGNK; the repeating Gly-X-Y sequence in collagen), and it had a molecular mass of 686.175 Da. It revealed that the anti-aging activity of GRRGNK was mainly due to skin protective effects. These results demonstrated that fish collagen hydrolysate may be a potential source of anti-aging peptides, which could be utilized in various field, including foods, cosmetics, and pharmaceuticals.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.38 no.4
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• pp.321-326
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• 2012

Recent studies have revealed that collagen peptide plays a protective role on skin by improving the activity of antioxidants and acts as an inducer of skin regeneration. To evaluate the efficacy of low molecular weight collagen peptide for skin recovery after non-ablative 1550 nm fractional photothermolysis laser. 10 volunteers were randomly divided into two groups. Both control and experimental groups received fractional photothermolysis treatment. In the experimental group, 5 subjects received oral collagen peptide 1,000 mg/day for 8 weeks. Before and after the treatment, we measured elastic recovery of skin, transepidermal water loss (TEWL) and erythema index (EI) for each patients. The evaluation of clinical results showed that elastic recovery of skin is higher in the experimental group than the control group (p < 0.05). TEWL have no significancy between two groups and erythema rapidly disappeared in the experimental group. On the quartile grading scale, the mean patient satisfaction 4 weeks after the fractional photothermolysis treatment was 2.0 in experimental group and 1.2 in control group. The low molecular weight collagen peptide appears to be an effective conservative therapy for skin recovery after non-ablative 1550 nm fractional photothermolysis treatment.