Identification of Matrix Metalloproteinase-1-Suppressive Peptides in Feather Keratin Hydrolysate

Hyeon Su Jin; Kyeongseop Song; Je Hyun Baek; Jae Eun Lee; Da Jeong Kim; Gae Won Nam; Nam Joo Kang; Dong Woo Lee

doi:10.1021/acs.jafc.8b05213

Identification of Matrix Metalloproteinase-1-Suppressive Peptides in Feather Keratin Hydrolysate

Hyeon Su Jin, Kyeongseop Song, Je Hyun Baek, Jae Eun Lee, Da Jeong Kim, Gae Won Nam, Nam Joo Kang, Dong Woo Lee

Department of Biotechnology

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

Inhibition of matrix metalloproteinases (MMPs), which degrade collagen and elastin in the dermis of normal skin, is a key strategy for anti-skin aging. In this study, we identified five low-molecular-weight (LMW, <1 kDa) MMP-1-suppressive peptides in feather keratin hydrolysate (FKH) obtained by anaerobic digestion with an extremophilic bacterium. FKH was first subjected to ultrafiltration, followed by size-exclusion chromatography and liquid chromatography/electrospray ionization tandem mass spectrometry analysis. Chemically synthesized peptides identical to the sequences identified suppressed MMP expression in human dermal fibroblasts (HDFs). To investigate the impact of the MMP-1-suppressive peptides on the signaling pathway, we performed antibody array phosphorylation profiling of HDFs. The results suggested that the peptide GGFDL regulates ultraviolet-B-induced MMP-1 expression by inhibiting mitogen-activated protein kinases and nuclear factor κB signaling pathways as well as histone modification. Thus, LMW feather keratin peptides could serve as novel bioactive compounds to protect the skin against intrinsic and extrinsic factors.

Original language	English
Pages (from-to)	12719-12729
Number of pages	11
Journal	Journal of Agricultural and Food Chemistry
Volume	66
Issue number	48
DOIs	https://doi.org/10.1021/acs.jafc.8b05213
Publication status	Published - 2018 Dec 5

Bibliographical note

Funding Information:
This work was supported by National Coordinating Center for Global Cosmetics R&D (NCR) Grant HN14C0097 to Nam Joo Kang, funded by the Ministry of Health and Welfare, National Research Foundation of Korea (NRF) Grants 2017R1A2B4005051 and 2017M3A9F3043852 to Dong-Woo Lee, funded by the Ministry of Science, Information and Communications Technology (ICT) and Future Planning, and Strategic Initiative for Microbiomes in Agriculture and Food Grant 918012-4 to Dong-Woo Lee, funded by the Ministry of Agriculture, Food, and Rural Affairs. Notes The authors declare no competing financial interest.

Publisher Copyright:
Copyright © 2018 American Chemical Society.

All Science Journal Classification (ASJC) codes

Chemistry(all)
Agricultural and Biological Sciences(all)

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10.1021/acs.jafc.8b05213

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title = "Identification of Matrix Metalloproteinase-1-Suppressive Peptides in Feather Keratin Hydrolysate",

abstract = "Inhibition of matrix metalloproteinases (MMPs), which degrade collagen and elastin in the dermis of normal skin, is a key strategy for anti-skin aging. In this study, we identified five low-molecular-weight (LMW, <1 kDa) MMP-1-suppressive peptides in feather keratin hydrolysate (FKH) obtained by anaerobic digestion with an extremophilic bacterium. FKH was first subjected to ultrafiltration, followed by size-exclusion chromatography and liquid chromatography/electrospray ionization tandem mass spectrometry analysis. Chemically synthesized peptides identical to the sequences identified suppressed MMP expression in human dermal fibroblasts (HDFs). To investigate the impact of the MMP-1-suppressive peptides on the signaling pathway, we performed antibody array phosphorylation profiling of HDFs. The results suggested that the peptide GGFDL regulates ultraviolet-B-induced MMP-1 expression by inhibiting mitogen-activated protein kinases and nuclear factor κB signaling pathways as well as histone modification. Thus, LMW feather keratin peptides could serve as novel bioactive compounds to protect the skin against intrinsic and extrinsic factors.",

author = "Jin, {Hyeon Su} and Kyeongseop Song and Baek, {Je Hyun} and Lee, {Jae Eun} and Kim, {Da Jeong} and Nam, {Gae Won} and Kang, {Nam Joo} and Lee, {Dong Woo}",

note = "Funding Information: This work was supported by National Coordinating Center for Global Cosmetics R&D (NCR) Grant HN14C0097 to Nam Joo Kang, funded by the Ministry of Health and Welfare, National Research Foundation of Korea (NRF) Grants 2017R1A2B4005051 and 2017M3A9F3043852 to Dong-Woo Lee, funded by the Ministry of Science, Information and Communications Technology (ICT) and Future Planning, and Strategic Initiative for Microbiomes in Agriculture and Food Grant 918012-4 to Dong-Woo Lee, funded by the Ministry of Agriculture, Food, and Rural Affairs. Notes The authors declare no competing financial interest. Publisher Copyright: Copyright {\textcopyright} 2018 American Chemical Society.",

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AU - Jin, Hyeon Su

AU - Song, Kyeongseop

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AU - Lee, Jae Eun

AU - Kim, Da Jeong

AU - Nam, Gae Won

AU - Kang, Nam Joo

AU - Lee, Dong Woo

N1 - Funding Information: This work was supported by National Coordinating Center for Global Cosmetics R&D (NCR) Grant HN14C0097 to Nam Joo Kang, funded by the Ministry of Health and Welfare, National Research Foundation of Korea (NRF) Grants 2017R1A2B4005051 and 2017M3A9F3043852 to Dong-Woo Lee, funded by the Ministry of Science, Information and Communications Technology (ICT) and Future Planning, and Strategic Initiative for Microbiomes in Agriculture and Food Grant 918012-4 to Dong-Woo Lee, funded by the Ministry of Agriculture, Food, and Rural Affairs. Notes The authors declare no competing financial interest. Publisher Copyright: Copyright © 2018 American Chemical Society.

PY - 2018/12/5

Y1 - 2018/12/5

N2 - Inhibition of matrix metalloproteinases (MMPs), which degrade collagen and elastin in the dermis of normal skin, is a key strategy for anti-skin aging. In this study, we identified five low-molecular-weight (LMW, <1 kDa) MMP-1-suppressive peptides in feather keratin hydrolysate (FKH) obtained by anaerobic digestion with an extremophilic bacterium. FKH was first subjected to ultrafiltration, followed by size-exclusion chromatography and liquid chromatography/electrospray ionization tandem mass spectrometry analysis. Chemically synthesized peptides identical to the sequences identified suppressed MMP expression in human dermal fibroblasts (HDFs). To investigate the impact of the MMP-1-suppressive peptides on the signaling pathway, we performed antibody array phosphorylation profiling of HDFs. The results suggested that the peptide GGFDL regulates ultraviolet-B-induced MMP-1 expression by inhibiting mitogen-activated protein kinases and nuclear factor κB signaling pathways as well as histone modification. Thus, LMW feather keratin peptides could serve as novel bioactive compounds to protect the skin against intrinsic and extrinsic factors.

AB - Inhibition of matrix metalloproteinases (MMPs), which degrade collagen and elastin in the dermis of normal skin, is a key strategy for anti-skin aging. In this study, we identified five low-molecular-weight (LMW, <1 kDa) MMP-1-suppressive peptides in feather keratin hydrolysate (FKH) obtained by anaerobic digestion with an extremophilic bacterium. FKH was first subjected to ultrafiltration, followed by size-exclusion chromatography and liquid chromatography/electrospray ionization tandem mass spectrometry analysis. Chemically synthesized peptides identical to the sequences identified suppressed MMP expression in human dermal fibroblasts (HDFs). To investigate the impact of the MMP-1-suppressive peptides on the signaling pathway, we performed antibody array phosphorylation profiling of HDFs. The results suggested that the peptide GGFDL regulates ultraviolet-B-induced MMP-1 expression by inhibiting mitogen-activated protein kinases and nuclear factor κB signaling pathways as well as histone modification. Thus, LMW feather keratin peptides could serve as novel bioactive compounds to protect the skin against intrinsic and extrinsic factors.

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Identification of Matrix Metalloproteinase-1-Suppressive Peptides in Feather Keratin Hydrolysate

Abstract

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