Publication :
Collagencin, an antibacterial peptide from fish collagen : activity, structure and interaction dynamics with membrane

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Date
2016-03-30
Direction de publication
Direction de recherche
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Éditeur
Elsevier
Projets de recherche
Structures organisationnelles
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Résumé

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.

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Revue
Biochemical and Biophysical Research Communications, Vol. 473 (2), 642–647 (2016)
DOI
10.1016/j.bbrc.2016.03.121
URL vers la version publiée
Mots-clés
Fish collagen, Collagencin, Antibacterial activity, Mechanism of action, Circular dichroism, Molecular dynamics
Citation
Licence CC
Type de document