Article ID Journal Published Year Pages File Type
3358399 International Journal of Antimicrobial Agents 2016 9 Pages PDF
Abstract

•A new antimicrobial from the whole body extract of the Brazilian Chilopoda Scolopendra viridicornis is described.•Lacrain presents specific activity against Gram-negative bacteria.•Lacrain is a peptide with a sequence of 8 amino acid residues (RYPAVGYT) and a molecular mass of 925.5 Da.•This peptide does not show cytotoxic activity against human erythrocytes.•This new molecule is the first described peptide with antimicrobial activity from the body extract of a myriapod.

Antimicrobial activities have previously been described by traditional Eastern medicine in Chilopoda body extracts, but until now no bioactive peptides have been described. In this study, a novel antimicrobial peptide, lacrain, was isolated from the body extract of the Brazilian Chilopoda Scolopendra viridicornis. The peptide was isolated by reverse-phase high-performance liquid chromatography (RP-HPLC). Its activity was tested using a liquid growth inhibition assay and the peptide was characterised using mass spectrometry. Lacrain has a sequence composed of eight amino acid residues and a molecular mass of 925.5 Da. A synthetic peptide of the native lacrain had identical characteristics to those of the isolated material, confirming its sequence. The synthetic peptide was active only against Gram-negative bacteria, showing strong bactericidal activity. Moreover, the peptide did not present haemolytic activity against human erythrocytes. Lacrain represents a novel molecule with powerful antibacterial activity that could be used as a new template for the development of drugs against clinically resistant bacterial strains.

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