Peptide name : Cecropin A

Source/Organism : Hybrid peptide

Linear/Cyclic : Not found

Chirality : Mix

Peptide length: 17

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Inhibition zone assay

Assay time : 48h

Activity : MIC : 0.125 - 32 mg/ml

Cell line : Not found

Cancer type : Not found

Other activity : Anti- microbial activity

Amino acid composition bar chart :

Molecular mass : 2177.72 Dalton

Aliphatic index : 0.747

Instability index : -14.411

Hydrophobicity (GRAVY) : -0.582

Isoelectric point : 10.778

Charge (pH 7) : 6.8403

Aromaticity : 0.235

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

Hydrophobic/hydrophilic ratio : 0.88888888

hydrophobic moment : -0.072

Missing amino acid : C,R,Q,T,P,M,E,D,Y,N,V,G

Most occurring amino acid : K

Most occurring amino acid frequency : 7

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.0, 0.4)

SMILES Notation: CC[C@H](C)[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)CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccccc1)C(=O)O

1 : Oh H, et al. Activities of synthetic hybrid peptides against anaerobic bacteria: aspects of methodology and stability. Antimicrob Agents Chemother. 2000; 44:68-72. doi: 10.1128/AAC.44.1.68-72.2000

Paper title : Activities of synthetic hybrid peptides against anaerobic bacteria: aspects of methodology and stability.

Doi : https://doi.org/10.1128/AAC.44.1.68-72.2000

Abstract : The increasing problem of antibiotic resistance among pathogenic bacteria requires development of new antimicrobial agents. One line of investigation is the synthesis of antimicrobial hybrid peptides. The aim of the present investigation was to determine the in vitro activities of 16 cecropin-melittin hybrid peptides (CAMEL analogues) against 60 anaerobic bacterial strains, to compare their activities with those of seven clinically used antimicrobial agents, and to compare different methods for anaerobic susceptibility testing of these peptides. The stability of one of the peptides, temporin B, with different stereoisomeric configurations was investigated in a fecal milieu. The CAMEL analogues showed antimicrobial activity against the anaerobic bacteria, with MICs ranging from 0.125 to 32 microg/ml. The overall activities (the MICs at which 90% of isolates are inhibited) of the CAMEL analogues against anaerobic bacteria were mainly inferior to those of imipenem, clindamycin, and piperacillin but were equal to or superior to those of metronidazole, cefoxitin, ciprofloxacin, and chloramphenicol. The agarose dilution method was found to be an accurate method for the testing of large numbers of bacterial strains. The D isomer of temporin B was inactivated more slowly in feces than the L isomer. This study shows that the CAMEL analogues are potential agents for the treatment of anaerobic infections.