Peptide name : Lt-MAP2

Source/Organism : Derivatives of Latarcin-3a

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 13

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Raji

Cancer type : Not found

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1630.1096 Dalton

Aliphatic index : 1.8

Instability index : -23.423

Hydrophobicity (GRAVY) : -0.007

Isoelectric point : 10.000

Charge (pH 7) : 3.7569

Aromaticity : 0.076

Molar extinction coefficient (cysteine, cystine): (1490, 1490)

Hydrophobic/hydrophilic ratio : 0.85714285

hydrophobic moment : 1.2588

Missing amino acid : C,R,W,H,Q,T,P,M,F,S,D,N,A,V,G

Most occurring amino acid : K

Most occurring amino acid frequency : 5

Least occurring amino acid : E

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.7, 0, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(C)C)[C@@H](C)CC)C(=O)O

1 : de Moraes LFRN, et al. First generation of multifunctional peptides derived from latarcin-3a from Lachesana tarabaevi spider toxin. Front Microbiol. 2022; 13:965621. doi: 10.3389/fmicb.2022.965621

Paper title : First generation of multifunctional peptides derived from latarcin-3a from Lachesana tarabaevi spider toxin.

Doi : https://doi.org/10.3389/fmicb.2022.965621

Abstract : The need for discovering new compounds that can act selectively on pathogens is becoming increasingly evident, given the number of deaths worldwide due to bacterial infections or tumor cells. New multifunctional biotechnological tools are being sought, including compounds present in spider venoms, which have high biotechnological potential. The present work aims to perform the rational design and functional evaluation of synthetic peptides derived from Lachesana tarabaevi spider toxin, known as latarcin-3a. The antimicrobial activity was tested against Gram-positive and -negative bacteria, with minimum inhibitory concentrations (MIC) between 4 and 128 μg.ml-1. Anti-biofilm tests were then performed to obtain MICs, where the peptides demonstrated activity from 4 to 128 μg.ml-1. In vitro cell cytotoxicity assays were carried out from tumor cell lines, lineages C1498, Kasumi-1, K-562, Jurkat, MOLT4, and Raji. Erythrocyte integrity was evaluated in the presence of synthetic peptides analog, which did not promote hemolysis at 128 μg.ml-1. The peptide that showed the best antibacterial activity was Lt-MAP3 and the best antitumor was Lt-MAP2. In conclusion, rational design of multifunctional antimicrobial peptides may be promising alternative tools in the treatment of emerging diseases such as bacterial infections and tumor cells.