• • DRAMP ID

  • DRAMP18213

• • Peptide Name

  • Gramicidin S(Bacteriocin)

• • Source

  • Bacillus brevis

• • Family

  • Not found

• • Gene

  • Not found

• • Sequence

  • VKLFPVKLFP

• • Sequence Length

  • 10

• • UniProt Entry

  • No entry found

• • Protein Existence

• • Biological Activity

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

• • Target Organism

  • Gram-positive, Gram-negative (broad-spectrum)

• • Hemolytic Activity

  • • It exhibits hemolytic activity at 25 μM and 45 μM against human red cells and sheep red cells.

• • Cytotoxicity

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

• • Binding Target

  • Cell membrane

• • Linear/Cyclic

  • Cyclic

• • N-terminal Modification

  • No specific N-terminal

• • C-terminal Modification

  • No specific C-terminal

• • Nonterminal Modifications and Unusual Amino Acids

  • The 'O' in sequence is Ornithine

• • Stereochemistry

  • Mixed(D-Phe)

• • Structure

  • Beta sheet

• • Structure Description

  • The second and seventh residues of this cyclic peptide are Ornithines, an analog of lysine (one CH2 shorter). They are represented here with lysines. In addition, residue F is a D-amino acid.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP18213.

DRAMP18213

• • Function

  • This is the first cyclic peptide antibiotic used clinically. For gram-negative bacteria, however, activity was strongly dependent on whether the assay was carried out in solution or in agar. It was found that GS was active against gram-negative microorganisms in the solution-based assay, but inactive against these using an agar-based assay. GS was also found to have antifungal activity when measured using a liquid-broth assay.

• ·Literature 1

• • Title

  • Gramicidin S is active against both gram-positive and gram-negative bacteria.

• • Pubmed ID

  • 8836773

• • Reference

  • Int J Pept Protein Res. 1996 Jun;47(6):460-6.

• • Author

  • Kondejewski LH, Farmer SW, Wishart DS, Hancock RE, Hodges RS.

• ·Literature 2

• • Title

  • Structure-activity relationships of the antimicrobial peptide gramicidin S and its analogs: aqueous solubility, self-association, conformation, antimicrobial activity and interaction with model lipid membranes.

• • Pubmed ID

  • 24388950

• • Reference

  • Biochim Biophys Acta. 2014 May;1838(5):1420-9.

• • Author

  • Abraham T, Prenner EJ, Lewis RN, Mant CT, Keller S, Hodges RS, McElhaney RN.