Peptide name : Crotamine

Source/Organism : Venom,South American rattlesnake

Linear/Cyclic : Not found

Chirality : L

Peptide length: 42

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Breast cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 4889.7772 Dalton

Aliphatic index : 0.185

Instability index : 82.6048

Hydrophobicity (GRAVY) : -1.095

Isoelectric point : 9.5064

Charge (pH 7) : 7.8701

Aromaticity : 0.119

Molar extinction coefficient (cysteine, cystine): (12490, 12865)

Hydrophobic/hydrophilic ratio : 1

hydrophobic moment : 0.4753

Missing amino acid : A,N,T,V

Most occurring amino acid : K

Most occurring amino acid frequency : 9

Least occurring amino acid : Y

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.3, 0.1)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CS)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)CNC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)Cc1ccc(O)cc1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)O

1 : Tang YQ, et al. Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes. Infect Immun. 1999; 67:6139-44. doi: 10.1128/IAI.67.11.6139-6144.1999

Paper title : Isolation, characterization, cDNA cloning, and antimicrobial properties of two distinct subfamilies of alpha-defensins from rhesus macaque leukocytes.

Doi : https://doi.org/10.1128/IAI.67.11.6139-6144.1999

Abstract : Experiments to isolate and characterize rhesus macaque myeloid alpha-defensins (RMADs) were conducted. Seven RMAD peptides were isolated and sequenced, and the cDNAs encoding six of these peptides and one other alpha-defensin from bone marrow were also characterized. Four of the RMADs were found to be highly similar to human neutrophil alpha-defensins HNP-1 to HNP-3, while the remaining four peptides were much more similar to human enteric alpha-defensin HD-5. Two alpha-defensin pairs differed only by the presence or absence of an additional arginine at the amino termini of their mature peptides, indicative of alternate posttranslational processing. The primary translation products of RMAD-1 to -8 are 94- and 96-amino-acid prepropeptides that are highly similar to those of human alpha-defensins. Immunolocalization experiments revealed a granular cytoplasmic pattern in the cytoplasms of neutrophils, indistinguishable from the pattern observed after immunostaining of human myeloid alpha-defensins in polymorphonuclear leukocytes. Each of the purified peptides was tested for its in vitro activities against Staphylococcus aureus 502a, Listeria monocytogenes EGD, Escherichia coli ML35, and Cryptococcus neoformans 271A. Several of the peptides were microbicidal for the gram-positive bacteria and C. neoformans at defensin concentrations in the range of 2 to 5 microM. All of the peptides were bacteriostatic against E. coli, but none were bactericidal for this organism. This study is the first to characterize the sequences and activities of alpha-defensins from nonhuman primates, data that should aid in delineating the role of these peptides in rhesus macaque host defense.