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Biochem Biophys Res Commun. 2016 Apr 29;473(2):642-7. doi: 10.1016/j.bbrc.2016.03.121. Epub 2016 Mar 30.

Collagencin, an antibacterial peptide from fish collagen: Activity, structure and interaction dynamics with membrane.

Author information

1
STELA Dairy Research Centre, Institute of Nutrition and Functional Foods, Université Laval, G1V 0A6 Québec, QC, Canada.
2
STELA Dairy Research Centre, Institute of Nutrition and Functional Foods, Université Laval, G1V 0A6 Québec, QC, Canada. Electronic address: riadh.hammami@fsaa.ulaval.ca.
3
Faculty of Pharmacy, Université Laval and Laboratory of Medicinal Chemistry, CHU de Québec Research Centre, G1V 4G2 Québec, QC, Canada.
4
STELA Dairy Research Centre, Institute of Nutrition and Functional Foods, Université Laval, G1V 0A6 Québec, QC, Canada; Department of Biology, Chemistry and Geography, Université du Québec à Rimouski (UQAR), 300 Allée des Ursulines, Rimouski, QC G5L 3A1, Canada. Electronic address: lucie.beaulieu@fsaa.ulaval.ca.
5
STELA Dairy Research Centre, Institute of Nutrition and Functional Foods, Université Laval, G1V 0A6 Québec, QC, Canada. Electronic address: ismail.fliss@fsaa.ulaval.ca.

Abstract

In this study, we first report characterization of collagencin, an antimicrobial peptide identified from fish collagen hydrolysate. The peptide completely inhibited the growth of Staphylococcus aureus at 1.88 mM. Although non-toxic up to 470 μM, collagencin was hemolytic at higher concentrations. The secondary structure of collagencin was mainly composed by β-sheet and β-turn as determined by CD measurements and molecular dynamics. The peptide is likely to form β-sheet structure under hydrophobic environments and interacts with both anionic (phosphatidylglycerol) and zwitterionic (phosphoethanolamine and phosphatidylcholine) lipids as shown with CD spectroscopy and molecular dynamics. The peptide formed several hydrogen bonds with both POPG and POPE lipids and remained at membrane-water interface, suggesting that collagencin antibacterial action follows a carpet mechanism. Collagenous fish wastes could be processed by enzymatic hydrolysis and transformed into products of high value having functional or biological properties. Marine collagens are a promising source of antimicrobial peptides with new implications in food safety and human health.

KEYWORDS:

Antibacterial activity; Circular dichroism; Collagencin; Fish collagen; Mechanism of action; Molecular dynamics

PMID:
27038545
DOI:
10.1016/j.bbrc.2016.03.121
[Indexed for MEDLINE]

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