Structure-Activity Relations of Myxinidin, an Antibacterial Peptide Derived from the Epidermal Mucus of Hagfish(942 views) Cantisani M, Leone M, Mignogna E, Kampanaraki K, Falanga A, Morelli G, Galdiero M, Galdiero S
Department of Pharmacy, CIRPEB and DFM, University of Naples Federico II, Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Naples, Italy
Center for Advanced Materials for Health Care IIT CRIB, Istituto Italiano di Tecnologia, Naples, Italy
Department of Experimental Medicine, II University of Naples, Naples, Italy
References: Not available.
Structure-Activity Relations of Myxinidin, an Antibacterial Peptide Derived from the 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, while insertion of arginine at charged and uncharged position increases antimicrobial activity compared with that of 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. Nuclear magnetic resonance (NMR) studies showed that myxinidin is able to form an amphipathic alpha-helical structure at the N terminus and a random coil region at the C terminus.
Structure-Activity Relations of Myxinidin, an Antibacterial Peptide Derived from the Epidermal Mucus of Hagfish
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Structure-Activity Relations of Myxinidin, an Antibacterial Peptide Derived from the Epidermal Mucus of Hagfish
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