Peptide name : Temporin-1Ga

Source/Organism : Synthetic

Linear/Cyclic : Linear

Chirality : L

Peptide length: 14

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : MTS assay

Assay time : Not Available

Activity : LC50 = 20 μM

Cell line : 4T1

Cancer type : Breast Cancer

Other activity : Antimicrobial

Amino acid composition bar chart :

Molecular mass : 1550.8786 Dalton

Aliphatic index : 1.528

Instability index : 24.6714

Hydrophobicity (GRAVY) : 1.5714

Isoelectric point : 8.4651

Charge (pH 7) : 0.4591

Aromaticity : 14.28

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

Hydrophobic/hydrophilic ratio : 1.8

hydrophobic moment : -1.725

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

Most occurring amino acid : S

Most occurring amino acid frequency : 3

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (21., 28., 64.)

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

1 : Mishra B, et al. Antibacterial, antifungal, anticancer activities and structural bioinformatics analysis of six naturally occurring temporins. Peptides. 2018; 106:9-20. doi: 10.1016/j.peptides.2018.05.011

Paper title : Antibacterial, antifungal, anticancer activities and structural bioinformatics analysis of six naturally occurring temporins.

Doi : https://doi.org/10.1016/j.peptides.2018.05.011

Abstract : Antimicrobial peptides are a special class of natural products with potential applications as novel therapeutics. This study focuses on six temporins (four with no activity data and two as positive controls). Using synthetic peptides, we report antibacterial, antifungal, and anticancer activities of temporins-CPa, CPb, 1Ga, 1Oc, 1Ola, and 1SPa. While temporin-1Ga and temporin-1OLa showed higher antifungal and anticancer activity, most of these peptides were active primarily against Gram-positive bacteria. Temporin-1OLa, with the highest cell selectivity index, could preferentially kill methicillin-resistant Staphylococcus aureus (MRSA), consistent with a reduced hemolysis in the presence of bacteria. Mechanistically, temporin-1OLa rapidly killed MRSA by damaging bacterial membranes. Using micelles as a membrane-mimetic model, we determined the three-dimensional structure of temporin-1OLa by NMR spectroscopy. The peptide adopted a two-domain structure where a hydrophobic patch is followed by a classic amphipathic helix covering residues P3-I12. Such a structure is responsible for anti-biofilm ability in vitro and in vivo protection of wax moths Galleria mellonella from staphylococcal infection. Finally, our bioinformatic analysis leads to a classification of temporins into six types and confers significance to this NMR structure since temporin-1OLa shares a sequence model with 62% of temporins. Collectively, our results indicate the potential of temporin-1OLa as a new anti-MRSA compound, which shows an even better anti-biofilm capability in combination with linezolid.