Structure activity relations of Myxinidin, an antibacterial peptide derived from Epidermal Mucus of Hagfish.

The structure activity relations of myxinidin a peptide derived from epidermal mucus of hagfish, Myxine glutinosa L. were investigated. Analysis of key residues allowed us to design new peptides with increased efficiency. Antimicrobial activity of native and modified peptides demonstrated the key role of uncharged residues in the sequence; the loss of these residues reduces almost entirely Myxinidin antimicrobial activity, whilst insertion of arginine at charged and uncharged position increases antimicrobial activity as compared with native myxinidin. Particularly, we designed a peptide capable of achieving a high inhibitory effect on bacterial growth. Experiments were conducted using both Gram-negative and Gram-positive bacteria. NMR studies showed that myxinidin is able to form an amphipathic α-helical structure at the N-terminus and a random coil region at the C-terminus.