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

Lars Erik Uggerhoj; Jens Kristian Munk; Paul R. Hansen; Peter Guentert; Reinhard Wimmer

doi:10.1016/j.febslet.2014.07.016

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

Lars Erik Uggerhoj, Jens Kristian Munk, Paul R. Hansen, Peter Guentert, Reinhard Wimmer

Research output: Contribution to journal › Journal article › Research › peer-review

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 alpha-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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Original language	English
Journal	F E B S Letters
Volume	588
Issue number	17
Pages (from-to)	3291-3297
Number of pages	7
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2014.07.016
Publication status	Published - 2014
Externally published	Yes

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title = "Structural features of peptoid-peptide hybrids in lipid-water interfaces",

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 alpha-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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.",

author = "Uggerhoj, {Lars Erik} and Munk, {Jens Kristian} and Hansen, {Paul R.} and Peter Guentert and Reinhard Wimmer",

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T1 - Structural features of peptoid-peptide hybrids in lipid-water interfaces

AU - Uggerhoj, Lars Erik

AU - Munk, Jens Kristian

AU - Hansen, Paul R.

AU - Guentert, Peter

AU - Wimmer, Reinhard

PY - 2014

Y1 - 2014

N2 - 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 alpha-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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

AB - 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 alpha-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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

U2 - 10.1016/j.febslet.2014.07.016

DO - 10.1016/j.febslet.2014.07.016

M3 - Journal article

C2 - 25063337

SN - 0014-5793

VL - 588

SP - 3291

EP - 3297

JO - F E B S Letters

JF - F E B S Letters

IS - 17

ER -

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

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