Membrane-disruptive abilities of beta-hairpin antimicrobial peptides correlate with conformation and activity: a 31P and 1H NMR study.

doi:10.1016/j.bbamem.2005.08.008

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Article

Membrane-disruptive abilities of beta-hairpin antimicrobial peptides correlate with conformation and activity: a 31P and 1H NMR study.

Biochimica et biophysica acta - 1 Oct 2005

Mani Rajeswari, Waring Alan J, Lehrer Robert I, Hong Mei

Abstract excerpt

The membrane interaction and solution conformation of two mutants of the beta-hairpin antimicrobial peptide, protegrin-1 (PG-1), are investigated to understand the structural determinants of antimicrobial potency. One mutant, [A(6,8,13,15)] PG-1, does not have the two disulfide bonds in wild-type PG-1, while the other, [Delta(4,18) G10] PG-1, has only half the number of cationic residues. 31P solid-state NMR...

Topics

Amino Acid Sequence
Anions
Antimicrobial Cationic Peptides
Cations
Cell Membrane
Escherichia coli
Glass
Lipid Bilayers
Lipids
Magnetic Resonance Spectroscopy
Membranes, Artificial
Models, Molecular
Molecular Conformation

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Molecular Sequence Data

Mutation

Peptides

Phosphorus Radioisotopes

Protein Conformation

Source

Open in PubMed

Identifiers

PMID: 16182236
DOI: 10.1016/j.bbamem.2005.08.008

Provenance

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