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

Lars Erik Uggerhøj; Jens K. Munk; Paul Robert Hansen; Peter Güntert; Reinhard Wimmer

doi:10.1016/j.febslet.2014.07.016

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

Lars Erik Uggerhøj, Jens K. Munk, Paul Robert Hansen, Peter Güntert, Reinhard Wimmer

6 Citations (Scopus)

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.

Original language	English
Journal	F E B S Letters
Volume	588
Issue number	17
Pages (from-to)	3291–3297
Number of pages	8
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2014.07.016
Publication status	Published - 25 Aug 2014

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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 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.",

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

AU - Uggerhøj, Lars Erik

AU - Munk, Jens K.

AU - Hansen, Paul Robert

AU - Güntert, Peter

AU - Wimmer, Reinhard

PY - 2014/8/25

Y1 - 2014/8/25

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 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.

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 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.

U2 - 10.1016/j.febslet.2014.07.016

DO - 10.1016/j.febslet.2014.07.016

M3 - Journal article

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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

Abstract

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