Peptide name : Temporin-ALa

Source/Organism : The rufous-spotted torrent frog, China, Asia

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 16

C-terminal modification: Not found

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : Not specified

Assay time : 24h

Activity : Not found

Cell line : HepG2

Cancer type : Not found

Other activity : Hemolytic activity

Amino acid composition bar chart :

Molecular mass : 1627.0193 Dalton

Aliphatic index : 1.887

Instability index : 0.1875

Hydrophobicity (GRAVY) : 1.625

Isoelectric point : 8.7501

Charge (pH 7) : 0.7591

Aromaticity : 0.062

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

Hydrophobic/hydrophilic ratio : 4.33333333

hydrophobic moment : 1.5886

Missing amino acid : C,R,W,H,Q,T,M,E,D,Y,N,A

Most occurring amino acid : L

Most occurring amino acid frequency : 6

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.3, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)Cc1ccccc1)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)O)C(C)C

1 : Lu Y, et al. Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis. Peptides. 2006; 27:3085-91. doi: 10.1016/j.peptides.2006.08.017

Paper title : Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis.

Doi : https://doi.org/10.1016/j.peptides.2006.08.017

Abstract : There are around 27 species of Amolops amphibian distributed in South-east of Asia. Seven antimicrobial peptides (AMPs) belonging to two different families were purified from skin of rufous-spotted torrent frog, Amolops loloensis, and designated brevinins-ALa, b, c, and d, and temporins-ALa, b, and c. The brevinins-AL family which is structurally related to brevinins-1 from skin secretions of the European frog, Rana brevipoda, is composed of 24 amino acids and has an intra-disulfide bridge at the C-terminus. The temporins-AL family, composed of 13 or 16 amino acid residues, is related with temporins from the skin secretions of R. temporaria. The findings of this study will facilitate the solutions to the taxonomic questions of the ranid genus Amolops and Staurois. In the work of this paper, both brevinins-ALb and temporin-Ma induced mast cell degranulation and histamine release, and had cytotoxic activity toward solid tumor cell line HepG(2). Brevinins-ALb also exerted strong hemolytic activity while temporin-Ma had no such activity.