Peptide name : Cecropin A

Source/Organism : Silkworm, Domestic silk moth

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 35

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 : Not found

Other activity : Anti-bacterial property

Amino acid composition bar chart :

Molecular mass : 3861.6286 Dalton

Aliphatic index : 1.142

Instability index : 31.24

Hydrophobicity (GRAVY) : -0.108

Isoelectric point : 11.166

Charge (pH 7) : 6.758

Aromaticity : 0.057

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 1.5

hydrophobic moment : 0.7771

Missing amino acid : C,H,T,M,Y

Most occurring amino acid : K

Most occurring amino acid frequency : 6

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.2, 0.3)

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

1 : Morishima I, et al. Isolation and structure of cecropins, inducible antibacterial peptides, from the silkworm, Bombyx mori. Comp Biochem Physiol B. 1990; 95:551-4. doi: 10.1016/0305-0491(90)90019-p

Paper title : Isolation and structure of cecropins, inducible antibacterial peptides, from the silkworm, Bombyx mori.

Doi : https://doi.org/10.1016/0305-0491(90)90019-p

Abstract : 1. Cecropins, inducible antibacterial peptides, were purified by simple two step chromatography from immunized larval hemolymph of the silkworm, Bombyx mori. 2. The cecropins were further separated into four major and two minor forms by reverse-phase HPLC. 3. The four major cecropins were sequenced and divided into two types, A and B, whose structures were quite similar to cecropins A and B of Hyalophora cecropia. 4. Three of them contained an unusual amino acid, delta-hydroxylysine. 5. No remarkable difference in antibacterial activity against E. coli was detected among these cecropins.