Employees – University of Copenhagen

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

Research output: Contribution to journalJournal articleResearchpeer-review

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

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 languageEnglish
JournalF E B S Letters
Volume588
Issue number17
Pages (from-to)3291–3297
Number of pages8
ISSN0014-5793
DOIs
Publication statusPublished - 2014

ID: 119771787