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

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

J Agric Food Chem. 2018 Dec 5;66(48):12719-12729.

PMID: 30395462

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4241275	Matrix Metalloproteinase-1 human			Price

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