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

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

Standard

Structural features of peptoid-peptide hybrids in lipid-water interfaces. / Uggerhøj, Lars Erik; Munk, Jens K.; Hansen, Paul Robert; Güntert, Peter; Wimmer, Reinhard.

In: F E B S Letters, Vol. 588, No. 17, 2014, p. 3291–3297.

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

Harvard

Uggerhøj, LE, Munk, JK, Hansen, PR, Güntert, P & Wimmer, R 2014, 'Structural features of peptoid-peptide hybrids in lipid-water interfaces', F E B S Letters, vol. 588, no. 17, pp. 3291–3297. https://doi.org/10.1016/j.febslet.2014.07.016

APA

Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P., & Wimmer, R. (2014). Structural features of peptoid-peptide hybrids in lipid-water interfaces. F E B S Letters, 588(17), 3291–3297. https://doi.org/10.1016/j.febslet.2014.07.016

Vancouver

Uggerhøj LE, Munk JK, Hansen PR, Güntert P, Wimmer R. Structural features of peptoid-peptide hybrids in lipid-water interfaces. F E B S Letters. 2014;588(17):3291–3297. https://doi.org/10.1016/j.febslet.2014.07.016

Author

Uggerhøj, Lars Erik ; Munk, Jens K. ; Hansen, Paul Robert ; Güntert, Peter ; Wimmer, Reinhard. / Structural features of peptoid-peptide hybrids in lipid-water interfaces. In: F E B S Letters. 2014 ; Vol. 588, No. 17. pp. 3291–3297.

Bibtex

@article{8218555a7f6d4548b8f541aba4277ff7,
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.",
author = "Uggerh{\o}j, {Lars Erik} and Munk, {Jens K.} and Hansen, {Paul Robert} and Peter G{\"u}ntert and Reinhard Wimmer",
year = "2014",
doi = "10.1016/j.febslet.2014.07.016",
language = "English",
volume = "588",
pages = "3291–3297",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "17",

}

RIS

TY - JOUR

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

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 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

C2 - 25063337

VL - 588

SP - 3291

EP - 3297

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 17

ER -

ID: 119771787