Balteatide – Antimicrobial Peptides – AMP

Balteatide is a novel antimicrobial peptide (AMP) isolated from the skin secretion of wild Peruvian purple-sided leaf frogs,-Phyllomedusa baltea. Balteatide has activity against the Gram-positive bacterium,-Staphylococcus aureus- the Gram-negative bacterium,-Escherichia coli- and the yeast,-Candida albicans- against which, unusually, it is most potent. Bateatide is also devoid of haemolytic activity up to concentrations of 512 mg/L. Balteatide is C-terminally amidated which is common in AMP as it effectively removes a membrane-repelling negative charge and replaces it with a hydrophobic membrane-interacting group. AMPs are a fundamental component of innate immunity/molecular defence across most forms of life and act in a membranolytic fashion to destroy the integrity of microorganisms. Balteatide differs from the myotropic peptide, sauvatide, by just one amino acid (I at position 9 in balteatide and T in sauvatide), however sauvatide displayed little or no antimicrobial activity and balteatide is devoid of myotropic activity.