Toll-like receptor agonist lipopeptides self-assemble into distinct nanostructures.
The self-assembled structure of toll-like receptor agonist lipopeptides containing the CSK4 peptide sequence is examined in aqueous solution. A remarkable dependence of morphology on the number of attached hexadecyl lipid chains is demonstrated, with spherical micelle structures for mono- and di-lipidated structures observed, but flexible wormlike micelles for the homologue containing three lipid chains. The distinct modes of assembly may have an important influence on the bioactivity of this class of lipopeptide.
Dept of Chemistry, University of Reading, Whiteknights Reading, RG6 6AD, UK. I.W.Hamley@reading.ac.uk.
Ian W
IW
Hamley
Steven
S
Kirkham
Ashkan
A
Dehsorkhi
Valeria
V
Castelletto
Mehedi
M
Reza
Janne
J
Ruokolainen
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D055666:Lipopeptides / Q000737:chemistry* / Q000378:metabolism; D049329:Nanostructures / Q000737:chemistry*; D011721:Pyrenes / Q000737:chemistry; D053838:Scattering, Small Angle; D051193:Toll-Like Receptors / Q000819:agonists* / Q000378:metabolism; D014867:Water / Q000737:chemistry; D014961:X-Ray Diffraction
D055666:Lipopeptides; D011721:Pyrenes; D051193:Toll-Like Receptors; D014867:Water; C030984:pyrene