Structure-activity relations of myxinidin, an antibacterial peptide derived from the epidermal mucus of hagfish.

Abstract:

: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 α-helical structure at the N terminus and a random coil region at the C terminus.

authors

Cantisani M,Leone M,Mignogna E,Kampanaraki K,Falanga A,Morelli G,Galdiero M,Galdiero S

doi

10.1128/AAC.01341-13

subject

Has Abstract

pub_date

2013-11-01 00:00:00

pages

5665-73

issue

11

eissn

0066-4804

issn

1098-6596

pii

AAC.01341-13

journal_volume

57

pub_type

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