• • DRAMP ID

  • DRAMP29096

• • Peptide Name

  • Collagencin

• • Source

  • Synthetic construct

• • Family

  • Not found

• • Gene

  • Not found

• • Sequence

  • GLPGPLGPAGPK

• • Sequence Length

  • 12

• • UniProt Entry

  • S4R4C8, S4R4C7, S4R4C5

• • Protein Existence

  • Predicted

• • Biological Activity

  • Antimicrobial, Antibacterial,Anti-Gram+, Anti-Gram-

• • Target Organism

  • • [Ref.27038545]32.2% growth inhibition on Listeria innocua HPB29 at 235 µM; 31% growth inhibition on Lactococcus lactis ATCC 11454 at 235 µM ; 32.2% growth inhibition on Carnobacterium divergens M35 at 235 µM; 67% growth inhibition on Staphylococcus aureus ATCC 6538 at 235 µM; 62% growth inhibition on Streptococcus pyogenes ATCC19615 at 235 µM; 64% growth inhibition on Escherichia coli MC4100 at 235 µM; Escherichia coli O157:H7(NA); Aeromonas hydrophila ATCC 7966(NA); Pseudomonas aeruginosa ATCC 27853(NA).

• • Hemolytic Activity

  • • [Ref.27038545]non-toxic to horse erythrocytes up to 470 μM; 25% hemolysis against horse erythrocytes at 940 µM.

• • Cytotoxicity

  • No cytotoxicity information found in the reference(s) presented

• • Binding Target

  • liposomes

• • Linear/Cyclic

  • Linear

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Free

• • Nonterminal Modifications and Unusual Amino Acids

  • None

• • Stereochemistry

  • L

• • Structure

  • Alpha helix,beta sheet,beta turn,random coil

• • Structure Description

  • The deconvolution of CD spectra in PBS buffer revealed that collagencin structure was organized as follow: 5.5% of α-helix, 19.3% of β-sheet, 36.3% of β-turn and 38.9% unordered. In methanol(organic buffers), a shift between β-sheet (36.4%) and β-turn (22.1%) was observed in collagencin structure while helix (4.9%) and unordered structure (36.6%) contents remained stables.In presence of DPPG phospholipids, a shift between β-sheet and β-turn was observed in collagencin structure. A maximal β-sheet content (49.7%) was observed at highest lipid: peptide ratio (100:1). In presence of POPG, α-helix

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP29096.

DRAMP29096

• • Function

  • Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.Collagencin highly interacts with both anionic and zwitterionic phospholipids but remains at membrane–water interface, which suggests a carpet mechanism of action of the peptide. Collagencin is probably antihypertensive according to its high similarity to peptide PGPLGLTGP, an ACE inhibitor that was previously isolated from skate skin hydrolysate.

• ·Literature 1

• • Title

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

• • Pubmed ID

  • 27038545

• • Reference

  • Biochem Biophys Res Commun. 2016 Apr 29;473(2):642-7.

• • Author

  • Ennaas N, Hammami R, Gomaa A, Bédard F, Biron É, Subirade M, Beaulieu L, Fliss I.