Peptide name : Kassiniatuerin-3

Source/Organism : Senegal running frog, Africa

Linear/Cyclic : Linear

Chirality : Not found

Peptide length: 20

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 24h

Activity : IC50 : 21.54 µM

Cell line : NCI-H157

Cancer type : Non-small cell Lung cancer

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 2313.78 Dalton

Aliphatic index : 1.61

Instability index : -1.87

Hydrophobicity (GRAVY) : 0.88

Isoelectric point : 6.9184

Charge (pH 7) : -0.0654

Aromaticity : 0.1

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

Hydrophobic/hydrophilic ratio : 2.33333333

hydrophobic moment : 1.086

Missing amino acid : C,R,W,T,M,E,S,Y,N,V

Most occurring amino acid : I

Most occurring amino acid frequency : 6

Least occurring amino acid : A

Least occurring amino acid frequency : 1

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

SMILES Notation: CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccccc1)C(=O)O)[C@@H](C)CC

1 : Wang H, et al. A Novel Antimicrobial Peptide (Kassinatuerin-3) Isolated from the Skin Secretion of the African Frog, Kassina senegalensis. Biology (Basel). 2020; 9:(unknown pages). doi: 10.3390/biology9070148

Paper title : A Novel Antimicrobial Peptide (Kassinatuerin-3) Isolated from the Skin Secretion of the African Frog, Kassina senegalensis.

Doi : https://doi.org/10.3390/biology9070148

Abstract : Amphibian skin secretions are remarkable sources of novel bioactive peptides. Among these, antimicrobial peptides have demonstrated an outstanding efficacy in killing microorganisms via a general membranolytic mechanism, which may offer the prospect of solving specific target-driven antibiotic resistance. Here, the discovery of a novel defensive peptide is described from the skin secretion of the African frog, Kassina senegalensis. Named kassinatuerin-3, it was identified through a combination of "shot-gun" cloning and MS/MS fragmentation sequencing. Subsequently, a synthetic replicate was subjected to biofunctional evaluation. The results indicated that kassinatuerin-3 possessed antimicrobial activity against Gram-positive bacteria but no effect against Gram-negative bacteria. Additionally, it was active in biofilm eradication on S. aureus and MRSA and in the antiproliferation of selected cancer cell lines. Moreover, it had a very mild hemolytic effect, which demonstrated a high therapeutic index for kassinatuerin-3. Collectively, although kassinatuerin-3 did not demonstrate remarkable bioactivities compared with other natural or synthetic antimicrobial peptides (AMPs), it offered a new insight into the design of antimicrobial derivatives.