General Information

    • DRAMP ID

    • DRAMP18193

    • Peptide Name

    • Cathelicidin-related peptide crotalicidin

    • Source

    • Crotalus durissus terrificus (South American rattlesnake)

    • Family

    • Belongs to the cathelicidin family.

    • Gene

    • N/A

    • Sequence

    • KRFKKFFKKVKKSVKKRLKKIFKKPMVIGVTIPF

    • Sequence Length

    • 34

    • Evidence code

    • N/A

Activity Information

    • Biological Activity

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

    • Target Organism

      • [Ref.25100358]Gram-negative: E.coli ATCC 25922 (MIC=0.25 μg/mL),P.aeruginosa (MIC=1 μg/mL);
      • Gram-positive: E.faecalis (MIC=32 μg/mL), S.aureus (MIC=32 μg/mL).

    • Hemolytic Activity

      • [Ref.25100358]10% hemolytic activity at 12.5 µM against red blood cells

    • Cytotoxicity

    • Binding Target

    • cell membrane

Structure Information

    • Linear/Cyclic/Branched

    • N-terminal modification

    • C-terminal modification

    • Other modifications

    • Stereochemistry

    • Structure

    • alpha helical

    • Structure Description

    • N/A

    • PDB ID

    • 2MWT resolved by NMR
    • DRAMP18193 helical wheel diagram
    • 2MWT-> 

Physical Information

    • Formula

    • C203H345N53O37S

    • Absent Amino Acids

    • ACDEHNQWY

    • Common Amino Acids

    • K

    • Mass

    • 474113

    • PI

    • 12.66

    • Basic Residues

    • 15

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 13

    • Boman Index

    • -5393

    • Hydrophobicity

    • -43.53

    • Aliphatic Index

    • 80

    • Half Life

      • Mammalian:1.3 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 3

DRAMP18193

DRAMP18193 chydropathy plot

Comments Information

    • Function

    • Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane (By similarity). Hemolytic activities have been observed on mammalian cells. Expressed by the venom gland.

Literature Information

  • Literature 1

    • Reference

    • Amino Acids 46:2561-2571(2014)

    • Author

    • Falcao C.B., de La Torre B.G., Perez-Peinado C., Barron A.E.,Andreu D., Radis-Baptista G.

    • Title

    • Vipericidins: a novel family of cathelicidin-related peptides fromthe venom gland of South American pit vipers.