Peptide name : Chaxapeptin

Source/Organism : Spore-forming, Gram-positive bacteria,"gifted" actinomycete strain C58; extremophile

Linear/Cyclic : Cyclic

Chirality : Not found

Peptide length: 15

C-terminal modification: Cyclic

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Cell invasion assay

Assay time : 36h

Activity : MIC : 50 μM

Cell line : A549

Cancer type : Lung cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1632.8117 Dalton

Aliphatic index : 0.52

Instability index : 7.1267

Hydrophobicity (GRAVY) : 0.2333

Isoelectric point : 5.8357

Charge (pH 7) : -0.2398

Aromaticity : 0.266

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

Hydrophobic/hydrophilic ratio : 2

hydrophobic moment : -0.369

Missing amino acid : C,R,W,H,Q,T,M,I,E,Y,A,V

Most occurring amino acid : F

Most occurring amino acid frequency : 4

Least occurring amino acid : K

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.5, 0.4)

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

1 : Elsayed SS, et al. Chaxapeptin, a Lasso Peptide from Extremotolerant Streptomyces leeuwenhoekii Strain C58 from the Hyperarid Atacama Desert. J Org Chem. 2015; 80:10252-60. doi: 10.1021/acs.joc.5b01878

Paper title : Chaxapeptin, a Lasso Peptide from Extremotolerant Streptomyces leeuwenhoekii Strain C58 from the Hyperarid Atacama Desert.

Doi : https://doi.org/10.1021/acs.joc.5b01878

Abstract : Lasso peptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) that possess a unique "lariat knot" structural motif. Genome mining-targeted discovery of new natural products from microbes obtained from extreme environments has led to the identification of a gene cluster directing the biosynthesis of a new lasso peptide, designated as chaxapeptin 1, in the genome of Streptomyces leeuwenhoekii strain C58 isolated from the Atacama Desert. Subsequently, 1 was isolated and characterized using high-resolution electrospray ionization mass spectrometry and nuclear magnetic resonance methods. The lasso nature of 1 was confirmed by calculating its nuclear Overhauser effect restraint-based solution structure. Chaxapeptin 1 displayed a significant inhibitory activity in a cell invasion assay with human lung cancer cell line A549.