Structural highlights
Publication Abstract from PubMed
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.
Structural features of peptoid-peptide hybrids in lipid-water interfaces.,Uggerhoj LE, Munk JK, Hansen PR, Guntert P, Wimmer R FEBS Lett. 2014 Aug 25;588(17):3291-7. doi: 10.1016/j.febslet.2014.07.016. Epub, 2014 Jul 22. PMID:25063337[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Uggerhoj LE, Munk JK, Hansen PR, Guntert P, Wimmer R. Structural features of peptoid-peptide hybrids in lipid-water interfaces. FEBS Lett. 2014 Aug 25;588(17):3291-7. doi: 10.1016/j.febslet.2014.07.016. Epub, 2014 Jul 22. PMID:25063337 doi:http://dx.doi.org/10.1016/j.febslet.2014.07.016
