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

    • Not found

    • Sequence

    • KRFKKFFKKVKKSVKKRLKKIFKKPMVIGVTIPF

    • Sequence Length

    • 34

    • Protein Existence

    • Not found

Activity Information

    • Biological Activity

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

    • 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] Crotalicidin reached 10% hemolysis at 25 μM. Even so, extrapolation of existing data indicates that 50% hemolysis would be reached at near-millimolar values, which defines an adequate (~2 log) selectivity window.

    • Cytotoxicity

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

    • Binding Target

    • cell membrane

Structure Information

    • Linear/Cyclic

    • Cyclic

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • None

    • Stereochemistry

    • L

    • Structure

    • alpha helical

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP18193 helical wheel diagram

    • PDB ID

    • 2MWT resolved by NMR
  • 2MWT-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP18193.

Physicochemical Information

    • Formula

    • C203H345N53O37S

    • Absent Amino Acids

    • ACDEHNQWY

    • Common Amino Acids

    • K

    • Mass

    • 4152.37

    • PI

    • 12.09

    • Basic Residues

    • 15

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 13

    • Net Charge

    • +15

    • Boman Index

    • -5393

    • Hydrophobicity

    • -0.435

    • 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

    • Title

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

    • 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.