Peptide name : Figainin 1

Source/Organism : Skin secretions, Chaco tree frog, South America

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 18

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 24h

Activity : IC50 : 10.5 µM

Cell line : B16F10

Cancer type : Leukemia

Other activity : Anti-bacterial property

Amino acid composition bar chart :

Molecular mass : 1916.3921 Dalton

Aliphatic index : 1.627

Instability index : -14.655

Hydrophobicity (GRAVY) : 1.4222

Isoelectric point : 10.002

Charge (pH 7) : 1.7581

Aromaticity : 0.111

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

Hydrophobic/hydrophilic ratio : 3.5

hydrophobic moment : -0.021

Missing amino acid : C,R,W,H,Q,M,E,S,D,Y,N,V

Most occurring amino acid : L

Most occurring amino acid frequency : 5

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.1, 0.6)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@@H](N)Cc1ccccc1)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCCN)C(=O)O)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)O

1 : Santana CJC, et al. Figainin 1, a Novel Amphibian Skin Peptide with Antimicrobial and Antiproliferative Properties. Antibiotics (Basel). 2020; 9:(unknown pages). doi: 10.3390/antibiotics9090625

Paper title : Figainin 1, a Novel Amphibian Skin Peptide with Antimicrobial and Antiproliferative Properties.

Doi : https://doi.org/10.3390/antibiotics9090625

Abstract : Amphibian skin secretions are abundant in bioactive compounds, especially antimicrobial peptides. These molecules are generally cationic and rich in hydrophobic amino acids, have an amphipathic structure and adopt an α-helical conformation when in contact with microorganisms membranes. In this work, we purified and characterized Figainin 1, a novel antimicrobial and antiproliferative peptide from the cutaneous secretion of the frog Boana raniceps. Figainin 1 is a cationic peptide with eighteen amino acid residues-rich in leucine and isoleucine, with an amidated C-terminus-and adopts an α-helical conformation in the presence of trifluoroethanol (TFE). It displayed activity against Gram-negative and especially Gram-positive bacteria, with MIC values ranging from 2 to 16 µM, and showed an IC₅₀ value of 15.9 µM against epimastigote forms of T. cruzi; however, Figanin 1 did not show activity against Candida species. This peptide also showed cytolytic effects against human erythrocytes with an HC₅₀ of 10 µM, in addition to antiproliferative activity against cancer cells and murine fibroblasts, with IC₅₀ values ranging from 10.5 to 13.7 µM. Despite its adverse effects on noncancerous cells, Figainin 1 exhibits interesting properties for the development of new anticancer agents and anti-infective drugs against pathogenic microorganisms.