Peptide name : Brevinin-1BYa

Source/Organism : Skin secretions, the foothill yellow-legged frog, North America

Linear/Cyclic : Not found

Chirality : L

Peptide length: 24

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti-bacterial activity; Anti-fungal activity

Amino acid composition bar chart :

Molecular mass : 2609.2849 Dalton

Aliphatic index : 1.220

Instability index : 26.5833

Hydrophobicity (GRAVY) : 1.075

Isoelectric point : 9.7013

Charge (pH 7) : 3.7363

Aromaticity : 0.125

Molar extinction coefficient (cysteine, cystine): (0, 125)

Hydrophobic/hydrophilic ratio : 3

hydrophobic moment : 0.2505

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

Most occurring amino acid : L

Most occurring amino acid frequency : 5

Least occurring amino acid : I

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.1, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)O)[C@@H](C)O)C(C)C

1 : Pál T, et al. Brevinin-1BYa: a naturally occurring peptide from frog skin with broad-spectrum antibacterial and antifungal properties. Int J Antimicrob Agents. 2006; 27:525-9. doi: 10.1016/j.ijantimicag.2006.01.010

Paper title : Brevinin-1BYa: a naturally occurring peptide from frog skin with broad-spectrum antibacterial and antifungal properties.

Doi : https://doi.org/10.1016/j.ijantimicag.2006.01.010

Abstract : Brevinin-1BYa (FLPILASLAAKFGPKLFCLVTKKC) is a cationic alpha-helical peptide containing an intramolecular disulphide bridge that is present in skin secretions of the foothill yellow-legged frog Rana boylii. A synthetic replicate of the peptide showed growth inhibitory activity against a range of reference strains of Gram-positive and Gram-negative bacteria, against clinical isolates of methicillin-resistant Staphylococcus aureus (MRSA) (minimum inhibitory concentration (MIC)=2.5 microM), and against reference strains and clinical isolates of the opportunistic yeast pathogens Candida albicans, Candida tropicalis, Candida krusei and Candida parapsilosis (MIC<or=10 microM). However, the therapeutic potential of the peptide, especially for systemic applications, is restricted by its high haemolytic activity against human erythrocytes (LD50=10 microM). Replacement of the cysteine residues in brevinin-1BYa by serine produced an acyclic analogue with eight-fold reduced haemolytic activity that retained high potency against Gram-positive bacteria, including strains of MRSA (MIC=5 microM), however activities against Gram-negative bacteria and yeast species were reduced. It is suggested that brevinin-1BYa represents a candidate for drug development, particularly for topical applications against antibiotic-resistant microorganisms.