Peptide name : Maximin H5

Source/Organism : Yunnan firebelly toad, China, Asia

Linear/Cyclic : Linear

Chirality : D

Peptide length: 20

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : Not specified

Assay time : 30min

Activity : MIC : 80 μM

Cell line : Not found

Cancer type : Not found

Other activity : Anti- microbial activity

Amino acid composition bar chart :

Molecular mass : 2022.3816 Dalton

Aliphatic index : 1.995

Instability index : 26.63

Hydrophobicity (GRAVY) : 1.48

Isoelectric point : 4.05

Charge (pH 7) : -3.2365

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 3

hydrophobic moment : 0.4148

Missing amino acid : C,R,W,H,Q,M,E,K,F,Y,N,A

Most occurring amino acid : L

Most occurring amino acid frequency : 6

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.4, 0.6)

SMILES Notation: CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)O)[C@@H](C)CC)C(C)C)[C@@H](C)O)C(C)C)C(C)C

1 : Lai R, et al. An anionic antimicrobial peptide from toad Bombina maxima. Biochem Biophys Res Commun. 2002; 295:796-9. doi: 10.1016/s0006-291x(02)00762-3

Paper title : An anionic antimicrobial peptide from toad Bombina maxima.

Doi : https://doi.org/10.1016/s0006-291x(02)00762-3

Abstract : Amphibian skin is a rich resource of antimicrobial peptides like maximins and maximins H from toad Bombina maxima. A novel cDNA clone encoding a precursor protein that comprises maximin 3 and a novel peptide, named maximin H5, was isolated from a skin cDNA library of B. maxima. The predicted primary structure of maximin H5 is ILGPVLGLVSDTLDDVLGIL-NH2. Containing three aspartate residues and no basic amino acid residues, maximin H5 is characterized by an anionic property. Different from cationic maximin H peptides, only Gram-positive strain Staphylococcus aureus was sensitive to maximin H5, while the other bacterial and fungal strains tested were resistant to it. The presence of metal ions, like Zn2+ and Mg2+, did not increase its antimicrobial potency. Maximin H5 represents the first example of potential anionic antimicrobial peptides from amphibians. The results provide the first evidence that, together with cationic antimicrobial peptides, anionic antimicrobial peptides may also exist naturally as part of the innate defense system.