General Information

    • DRAMP ID

    • DRAMP01085

    • Peptide Name

    • Alyteserin-1c (toads, amphibians, animals)

    • Source

    • Alytes obstetricans (Common midwife toad) (Bufo obstetricans)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • GLKEIFKAGLGSLVKGIAAHVAS

    • Sequence Length

    • 23

    • Protein Existence

    • Protein level

    • SMILES

    • CC[C@@H](C)[C@H](NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)CN)[C@H](C)CC)C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(N)=O)C(C)C

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-

    • Target Organism

      • Gram-negative bacterium:
        Target OrganismActivity
        Escherichia coliMIC=25 µM

    • Hemolytic Activity

      • [Ref:19463738] LC50 = 145 μM against human erthrocytes.

    • Cytotoxicity

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

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • α-Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • Stereochemistry

    • L (to be determined)

    • Structure

    • Alpha helix

    • Structure Description

    • Solution structural studies in the membrane mimicking environments, sodium dodecyl sulphate (SDS), dodecylphosphocholine (DPC), and 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine (DHPC) micelles, indicate that these peptides display an alpha helical structure between residues Lys(3) and Val(21).(Ref.1)

    • PDB ID

    • 2L5R resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP01085.

Physicochemical Information

    • Formula

    • C104H176N28O28

    • Absent Amino Acids

    • CDMNPQRTWY

    • Common Amino Acids

    • AG

    • Mass

    • 2266.71

    • PI

    • 9.7

    • Basic Residues

    • 4

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 12

    • Net Charge

    • +3

    • Boman Index

    • 11.74

    • Hydrophobicity

    • 0.748

    • Aliphatic Index

    • 127.39

    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 6

DRAMP01085

Comments Information

    • Function

    • Alyteserin-1c shows selective growth-inhibitory activity against Gram-negative bacteria.

Literature Information

  • ·Literature 1

    • Title

    • Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c.

    • Reference

    • Biochim Biophys Acta. 2011 Aug;1808(8):1975-1984.

    • Author

    • Subasinghage AP, O'Flynn D, Conlon JM, Hewage CM.
  • ·Literature 2

    • Title

    • The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae).

    • Reference

    • Peptides. 2009 Jun;30(6):1069-1073.

    • Author

    • Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC.