Peptide name : Emericellipsin A

Source/Organism : Emericellopsis alkaline** VKPM F1428, Alkalophile, extremophile

Linear/Cyclic : Linear

Chirality : Mix

Peptide length: 9

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 72h

Activity : EC50 : 2.8 µM

Cell line : Hep G2

Cancer type : Liver cancer

Other activity : Anti-microbial activity; Anti-fungal activity

Amino acid composition bar chart :

Molecular mass : 812.9106 Dalton

Aliphatic index : 1.088

Instability index : 20.8556

Hydrophobicity (GRAVY) : 0.8667

Isoelectric point : 5.955

Charge (pH 7) : -0.0415

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 3.5

hydrophobic moment : -0.363

Missing amino acid : C,R,W,H,T,M,E,K,F,D,Y,L,N

Most occurring amino acid : A

Most occurring amino acid frequency : 3

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.2)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H]1CCCN1)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)NCC(=O)O)C(C)C

1 : Rogozhin EA, et al. A Novel Lipopeptaibol Emericellipsin A with Antimicrobial and Antitumor Activity Produced by the Extremophilic Fungus Emericellopsis alkalina. Molecules. 2018; 23:(unknown pages). doi: 10.3390/molecules23112785

Paper title : A Novel Lipopeptaibol Emericellipsin A with Antimicrobial and Antitumor Activity Produced by the Extremophilic Fungus Emericellopsis alkalina.

Doi : https://doi.org/10.3390/molecules23112785

Abstract : Soil fungi are known to contain a rich variety of defense metabolites that allow them to compete with other organisms (fungi, bacteria, nematodes, and insects) and help them occupy more preferential areas at the expense of effective antagonism. These compounds possess antibiotic activity towards a wide range of other microbes, particularly fungi that belong to different taxonomical units. These compounds include peptaibols, which are non-ribosomal synthesized polypeptides containing non-standard amino acid residues (alpha-aminoisobutyric acid mandatory) and some posttranslational modifications. We isolated a novel antibiotic peptide from the culture medium of Emericellopsis alkalina, an alkalophilic strain. This peptide, called emericellipsin A, exhibited a strong antifungal effect against the yeast Candida albicans, the mold fungus Aspergillus niger, and human pathogen clinical isolates. It also exhibited antimicrobial activity against some Gram-positive and Gram-negative bacteria. Additionally, emericellipsin A showed a significant cytotoxic effect and was highly active against Hep G2 and HeLa tumor cell lines. We used NMR spectroscopy to reveal that this peptaibol is nine amino acid residues long and contains non-standard amino acids. The mode of molecular action of emericellipsin A is most likely associated with its effects on the membranes of cells. Emericellipsin A is rather short peptaibol and could be useful for the development of antifungal, antibacterial, or anti-tumor remedies.