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

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. - Highlights: • Collagencin, an antibacterial (G+ & G-) peptide identified from fish collagen hydrolysate. • The peptide completely inhibited the growth of S. aureus at 1.88 mM and non-toxic at 470 μM. • The secondary structure was mainly composed by β-sheet and turn as determined by CDmore » and MD. • Collagencin interacts with both anionic and zwitterionic lipids as shown with CD and MD. • Collagencin antibacterial action probably follows a carpet mechanism.« less

Authors:
 [1];  [1];  [1]; ;  [2];  [1];  [1];  [3];  [1]
  1. STELA Dairy Research Centre, Institute of Nutrition and Functional Foods, Université Laval, G1V 0A6 Québec, QC (Canada)
  2. Faculty of Pharmacy, Université Laval and Laboratory of Medicinal Chemistry, CHU de Québec Research Centre, G1V 4G2 Québec, QC (Canada)
  3. (UQAR), 300 Allée des Ursulines, Rimouski, QC G5L 3A1 (Canada)
Publication Date:
OSTI Identifier:
22596371
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 473; Journal Issue: 2; Other Information: Copyright (c) 2016 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ABUNDANCE; COLLAGEN; CONCENTRATION RATIO; DICHROISM; ENZYMATIC HYDROLYSIS; FOOD; LECITHINS; MEMBRANES; MOLECULAR DYNAMICS METHOD; PEPTIDES; PUBLIC HEALTH; SAFETY; SPECTROSCOPY; STAPHYLOCOCCUS; TOXICITY; ZWITTERIONIC COMPOUNDS

Citation Formats

Ennaas, Nadia, Hammami, Riadh, E-mail: riadh.hammami@fsaa.ulaval.ca, Gomaa, Ahmed, Bédard, François, Biron, Éric, Subirade, Muriel, Beaulieu, Lucie, E-mail: lucie.beaulieu@fsaa.ulaval.ca, Department of Biology, Chemistry and Geography, Université du Québec à Rimouski, and Fliss, Ismail, E-mail: ismail.fliss@fsaa.ulaval.ca. Collagencin, an antibacterial peptide from fish collagen: Activity, structure and interaction dynamics with membrane. United States: N. p., 2016. Web. doi:10.1016/J.BBRC.2016.03.121.
Ennaas, Nadia, Hammami, Riadh, E-mail: riadh.hammami@fsaa.ulaval.ca, Gomaa, Ahmed, Bédard, François, Biron, Éric, Subirade, Muriel, Beaulieu, Lucie, E-mail: lucie.beaulieu@fsaa.ulaval.ca, Department of Biology, Chemistry and Geography, Université du Québec à Rimouski, & Fliss, Ismail, E-mail: ismail.fliss@fsaa.ulaval.ca. Collagencin, an antibacterial peptide from fish collagen: Activity, structure and interaction dynamics with membrane. United States. doi:10.1016/J.BBRC.2016.03.121.
Ennaas, Nadia, Hammami, Riadh, E-mail: riadh.hammami@fsaa.ulaval.ca, Gomaa, Ahmed, Bédard, François, Biron, Éric, Subirade, Muriel, Beaulieu, Lucie, E-mail: lucie.beaulieu@fsaa.ulaval.ca, Department of Biology, Chemistry and Geography, Université du Québec à Rimouski, and Fliss, Ismail, E-mail: ismail.fliss@fsaa.ulaval.ca. Fri . "Collagencin, an antibacterial peptide from fish collagen: Activity, structure and interaction dynamics with membrane". United States. doi:10.1016/J.BBRC.2016.03.121.
@article{osti_22596371,
title = {Collagencin, an antibacterial peptide from fish collagen: Activity, structure and interaction dynamics with membrane},
author = {Ennaas, Nadia and Hammami, Riadh, E-mail: riadh.hammami@fsaa.ulaval.ca and Gomaa, Ahmed and Bédard, François and Biron, Éric and Subirade, Muriel and Beaulieu, Lucie, E-mail: lucie.beaulieu@fsaa.ulaval.ca and Department of Biology, Chemistry and Geography, Université du Québec à Rimouski and Fliss, Ismail, E-mail: ismail.fliss@fsaa.ulaval.ca},
abstractNote = {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. - Highlights: • Collagencin, an antibacterial (G+ & G-) peptide identified from fish collagen hydrolysate. • The peptide completely inhibited the growth of S. aureus at 1.88 mM and non-toxic at 470 μM. • The secondary structure was mainly composed by β-sheet and turn as determined by CD and MD. • Collagencin interacts with both anionic and zwitterionic lipids as shown with CD and MD. • Collagencin antibacterial action probably follows a carpet mechanism.},
doi = {10.1016/J.BBRC.2016.03.121},
journal = {Biochemical and Biophysical Research Communications},
number = 2,
volume = 473,
place = {United States},
year = {Fri Apr 29 00:00:00 EDT 2016},
month = {Fri Apr 29 00:00:00 EDT 2016}
}