• BMB Reports
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• v.53 no.10
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• pp.539-544
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• 2020

Skin aging appears to be the result of overlapping intrinsic (including genetic and hormonal factors) and extrinsic (external environment including chronic light exposure, chemicals, and toxins) processes. These factors cause decreases in the synthesis of collagen type I and elastin in fibroblasts and increases in the melanin in melanocytes. Collagen Type I is the most abundant type of collagen and is a major structural protein in human body tissues. In previous studies, many products containing collagen derived from land and marine animals as well as other sources have been used for a wide range of purposes in cosmetics and food. However, to our knowledge, the effects of human collagen-derived peptides on improvements in skin condition have not been investigated. Here we isolate and identify the domain of a human COL1A2-derived protein which promotes fibroblast cell proliferation and collagen type I synthesis. This human COL 1A2-derived peptide enhances wound healing and elastin production. Finally, the human collagen alpha-2 type I-derived peptide (SMM) ameliorates collagen type I synthesis, cell proliferation, cell migration, and elastin synthesis, supporting a significant anti-wrinkle effect. Collectively, these results demonstrate that human collagen alpha-2 type I-derived peptides is practically accessible in both cosmetics and food, with the goal of improving skin condition.

• Food Science of Animal Resources
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• v.39 no.6
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• pp.966-979
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• 2019

Muscle-based by-products are often undervalued although commonly reported having a high amount of natural bioactive peptides. In this study, elastin was isolated from the protein of broiler hen skin while its hydrolysate was prepared using Elastase. Assessment of antioxidative properties of elastin-based hydrolysate (EBH) was based on three different assays; 2,2-diphenyl-1-picryl-hydrazyl-hydrate (DPPH) radical, 2,2'-azinobis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) radical and metal chelating ability. The EBH was purified further using ultrafiltration, gel filtration and Reverse- Phase High-Performance Liquid Chromatography (RP-HPLC). The IC₅₀ of ABTS radical activities for EBH were decreased as EBH further purified using ultrafiltration (EBH III; 0.66 mg/mL)>gel filtration (EB-II; 0.42 mg/mL)>RP-HPLC (EB-II4; 0.12 mg/mL). The sequential identification of the peptide was done by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry (MALDI-TOF/ TOF-MS) of the potent fractions obtained from RP-HPLC (EB-II4). The presence of hydrophobic amino acids (Val and Pro) in the peptide sequences could potentially contribute to the high antioxidant activity of EBH. The sequences GAHTGPRKPFKPR, GMPGFDVR and ADASVLPK were identified as antioxidant peptides. In conclusion, the antioxidative potential from poultry skin specifically from elastin is evident and can be explored to be used in many applications such as health and pharmaceutical purposes.

• Polymer(Korea)
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• v.35 no.3
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• pp.223-227
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• 2011

Stimuli-responsive polymers have been investigated as the materials playing the critical roles in various applications. Thermoresponsive graft copolymers, poly (N-isopropylacrylamide)-g-hyaluronic acid (PNIPAAm-g-HA) and elastin-like peptide-g-hyaluronic acid (ELP-g-HA), were synthesized by coupling carboxylic polymers (PNIPAAm-COOH or ELP) to biocompatible HA through amide linkages. Thermoresponsive behavior was observed in both the copolymers, and the results of turbidity measurement were consistent with the results of rheological examination. Among the two copolymers, the ELP graft copolymer shows less cooperative LCST transition than the PNIPAAm case. As the content of graft chains of PNIPAAm and ELP increases, viscosity increases, and the increase was larger in PNIPAAm case at a graft content. These results shows us that the introduction of grafts provides thermosensitivity to biocompatible HA, whose characteristics can be engineered.

• Biomedical Science Letters
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• v.19 no.1
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• pp.41-47
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• 2013

Pluripotent stem cells (PSCs) have lots of potential in biomedical sciences owing to its potential to differentiate into any kind of cells in the body. However, it is still a challenge to culture PSCs on a large scale for application to regenerative medicine. Herein, we introduce a synthetic polymer that enables large-scale suspension culture of human PSCs. By employing suspension culture, it became unnecessary to use conventional substrata such as mouse embryonic fibroblast (MEF) or Matrigel$^{TM}$, which are believed to be main causative sources of xenogeneic contamination in cultured human PSCs in vitro. Human PSCs were cultured in the medium in which elastin-like polypeptide (ELP) dissolved. The ELP in the medium became harden as temperature increases by transforming the medium into a semi-solid gel that supported growth of human PSCs in suspension. Gel-sol transition temperature of ELP can be adjusted by modifying the peptide sequence in which 5 amino acids, Val-Pro-Gly-Xaa-Gly, repeated sequentially. We constructed 3D suspension media having transition temperature around $33{\sim}35^{\circ}C$ using an ELP consisted of 40, 60, or 80 repeats of a monomer, which was Val-Pro-Gly-Val-Gly. Among the ELPs, ELP80 was chosen as the best ELP to support growth of human PSCs in suspension culture. This result suggests that the ELP80 can be a medium component for culturing human PSCs in large-scale.

• Korean Journal of Food Science and Technology
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• v.41 no.4
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• pp.441-445
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• 2009

Recent research has revealed that hydrolyzed collagen peptides have beneficial effects in various diseases such as osteoarthritis and human rheumatoid arthritis and also play a protective role in skin by improving the activity of antioxidants. In this study, we investigated the effects of a novel mixture (AP-CPM01) containing collagen peptides and elastin peptides on photoaged hairless mice skin both in vivo and in vitro. To evaluate the effects of AP-CPM01 on UVBinduced skin wrinkle formation in vivo, the hairless mice were exposed to UVB irradiation and orally administered the AP-CPM01 at 333 mg/kg per day for 10 weeks. The effects on skin appearance and epidermal thickness were measured using bioengineering and histochemical methods. In addition, the influence of AP-CPM01 on collagen metabolism in human skin fibroblasts was also investigated. The skin of mice in the AP-CPM01 treated group had better appearance and less wrinkling than that of mice in the control group. In the human fibroblast cells, the amount of de novo procollagen synthesis was increased after AP-CPM01 treatment, reflecting that AP-CPM01 can induce de novo procollagen synthesis and reduce UVB-induced skin wrinkle formation. These results suggest that AP-CPM01 is a potent candidate for antiphotoaging functions.

• 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.

• The Korea Journal of Herbology
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• v.29 no.1
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• pp.7-12
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• 2014

Objectives : Polygoni Multiflori Radix (PMR), the roots of Polygonum multiflorum Thunberg, is used to nourish the blood and yin and used for preventing premature greying of the hair. There are some articles on its preventing effects on the melanogenesis. However, there is no report about its effects on the collagen and elastin. The present study was designed to investigate its effects on collagen metabolism and elastase activity. Methods : The effects of PMR on type I procollagen production and collagenase activity in human normal fibroblasts Hs68 after UVB (312 nm) irradiation were measured by ELISA method. Cells were pretreated with the PMR for 24 hours prior to UVB irradiation. After UVB irradiation, cells were retreated with the sample and incubated for additional 24 hours. The amount of collagen type I was measured with a procollagen type I C-peptide assay kit. The activity of collagenase was measured with a MMP-1 human biotrak ELISA system. The elastase activities after treatment of PMR were measured as well. Results : In the present study, the collagen production was not increased. However, the increased collagenase activity after UVB damage was significantly recovered to $50.2{\pm}14.5%$, $8.2{\pm}3.1%$, and $10.0{\pm}3.3%$ (10, 30, and $100{\mu}g/ml$). The elastase activities (10, 100, and $1000{\mu}g/ml$) significantly reduced to $75.2{\pm}5.2%$, $40.3{\pm}1.2%$, and $27.0{\pm}1.9%$, respectively. Conclusion : PMR showed the inhibitory effects on collagenase and elastase activity. These results suggest that PMR may have potential as an anti-aging ingredient in cosmetic herbal treatment.