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FEBS Lett. 2014 Aug 25;588(17):3291-7. doi: 10.1016/j.febslet.2014.07.016. Epub 2014 Jul 22.

Structural features of peptoid-peptide hybrids in lipid-water interfaces.

Author information

1
Department of Biotechnology, Chemistry, and Environmental Engineering, Aalborg University, Sohngaardsholmsvej 49, 9000 Aalborg, Denmark.
2
Department of Drug Design and Pharmacology, University of Copenhagen, Universitetsparken 2, 2100 Copenhagen, Denmark.
3
Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, J. W. Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany.
4
Department of Biotechnology, Chemistry, and Environmental Engineering, Aalborg University, Sohngaardsholmsvej 49, 9000 Aalborg, Denmark. Electronic address: rw@bio.aau.dk.

Abstract

The inclusion of peptoid monomers into antimicrobial peptides (AMPs) increases their proteolytic resistance, but introduces conformational flexibility (reduced hydrogen bonding ability and cis/trans isomerism). We here use NMR spectroscopy to answer how the insertion of a peptoid monomer influences the structure of a regular α-helical AMP upon interaction with a dodecyl phosphocholine (DPC) micelle. Insertion of [(2-methylpropyl)amino]acetic acid in maculatin-G15 shows that the structural change and conformational flexibility depends on the site of insertion. This is governed by the micelle interaction of the amphipathic helices flanking the peptoid monomer and the side chain properties of the peptoid and its preceding residue.

KEYWORDS:

Antimicrobial peptides; Maculatin; NMR; Paramagnetic relaxation enhancement; Peptoids

PMID:
25063337
DOI:
10.1016/j.febslet.2014.07.016
[Indexed for MEDLINE]
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