Peptide name : XLAsp-P1

Source/Organism : Skin, African clawed frog, Africa

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 5

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 24h

Activity : LC50 : < 5 μg/mL

Cell line : MCF-7 cells

Cancer type : Breast cancer

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 607.4789 Dalton

Aliphatic index : 0

Instability index : 46.52

Hydrophobicity (GRAVY) : -3.5

Isoelectric point : 4.05

Charge (pH 7) : -5.2294

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 0

hydrophobic moment : -0.806

Missing amino acid : W,T,P,I,M,K,F,N,G,C,R,H,Q,S,Y,L,A,V

Most occurring amino acid : D

Most occurring amino acid frequency : 4

Least occurring amino acid : E

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.8, 0)

SMILES Notation: N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O

1 : Li S, et al. A novel short anionic antibacterial peptide isolated from the skin of Xenopus laevis with broad antibacterial activity and inhibitory activity against breast cancer cell. Arch Microbiol. 2016; 198:473-82. doi: 10.1007/s00203-016-1206-8

Paper title : A novel short anionic antibacterial peptide isolated from the skin of Xenopus laevis with broad antibacterial activity and inhibitory activity against breast cancer cell.

Doi : https://doi.org/10.1007/s00203-016-1206-8

Abstract : A vastarray of bioactive peptides from amphibian skin secretions is attracting increasing attention due to the growing problem of bacteria resistant to conventional antibiotics. In this report, a small molecular antibacterial peptide, named Xenopus laevis antibacterial peptide-P1 (XLAsp-P1), was isolated from the skin of Xenopus laevis using reversed-phase high-performance liquid chromatography. The primary structure of XLAsp-P1, which has been proved to be a novel peptide by BLAST search in AMP database, was DEDDD with a molecular weight of 607.7 Da analysed by Edman degradation and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/TOF-MS). The highlight of XLAsp-P1 is the strong in vitro potency against a variety of Gram-positive and Gram-negative bacteria with minimum inhibitory concentrations (MICs) starting at 10 μg/mL and potent inhibitory activity against breast cancer cell at tested concentrations from 5 to 50 μg/mL. In addition, only 6.2 % of red blood cells was haemolytic when incubated with 64 μg/mL (higher than MICs of all bacterial strain) of XLAsp-P1. The antimicrobial mechanism for this novel peptide was the destruction of the cell membrane investigated by transmission electron microscopy. All these showed that XLAsp-P1 is a novel short anionic antibacterial peptide with broad antibacterial activity and inhibitory activity against breast cancer cell.