Peptide name : Tritrpticin

Source/Organism : Pig

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 13

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MIC assay

Assay time : 18h

Activity : MIC : 2 mM

Cell line : Not found

Cancer type : Not found

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 1902.2544 Dalton

Aliphatic index : 0.523

Instability index : 139.584

Hydrophobicity (GRAVY) : -0.792

Isoelectric point : 12

Charge (pH 7) : 3.7339

Aromaticity : 0.384

Molar extinction coefficient (cysteine, cystine): (16500, 16500)

Hydrophobic/hydrophilic ratio : 2.25

hydrophobic moment : 0.4063

Missing amino acid : C,H,Q,T,M,I,E,K,S,D,Y,N,A,G

Most occurring amino acid : R

Most occurring amino acid frequency : 4

Least occurring amino acid : V

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.0, 0.1, 0.5)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](N)C(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O

1 : Lawyer C, et al. Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides. FEBS Lett. 1996; 390:95-8. doi: 10.1016/0014-5793(96)00637-0

Paper title : Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides.

Doi : https://doi.org/10.1016/0014-5793(96)00637-0

Abstract : It has long been speculated that porcine cathelin is an N-terminal fragment of a longer precursor protein which possesses antimicrobial activity. In an attempt to find such a precursor, a cDNA clone was recently isolated and sequenced by screening a cDNA library from porcine bone marrow. In order to identify the functional activity of the putative protein encoded by an open reading frame, we have synthesized various lengths of peptides that correspond to the C-terminal region of the protein and examined them for their antimicrobial activities. We found that a 13 amino acid tryptophan-rich region with the sequence of VRRFPWWWPFLRR had strong antimicrobial activity with a wide spectrum. It showed potency against Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumonia, Staphylococcus epidermidis, Proteus mirabilis, and Streptococcus group D as well as Aspergillus fumigatus. The action of this peptide is bactericidal rather than bacteriostatic and this activity is completely inhibited by 2 mM MgCl2. Our results indicate that the previously identified putative precursor encoded by the isolated cDNA indeed possesses a potent antimicrobial activity and that this 13 amino acid synthetic peptide is considered to be a potentially effective drug against various infectious agents.