| 1. |
- König, Nico, et al.
(författare)
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Spherical Micelles with Nonspherical Cores : Effect of Chain Packing on the Micellar Shape
- 2020
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Ingår i: Macromolecules. - : American Chemical Society (ACS). - 0024-9297 .- 1520-5835. ; , s. 10686-10698
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Tidskriftsartikel (refereegranskat)abstract
- Self-assembly of amphiphilic polymers into micelles is an archetypical example of a "self-confined"system due to the formation of micellar cores with dimensions of a few nanometers. In this work, we investigate the chain packing and resulting shape of Cn-PEOx micelles with semicrystalline cores using small/wide-angle X-ray scattering (SAXS/WAXS), contrast-variation small-angle neutron scattering (SANS), and nuclear magnetic resonance spectroscopy (NMR). Interestingly, the n-alkyl chains adopt a rotator-like conformation and pack into prolate ellipses (axial ratio ϵ ≈ 0.5) in the "crystalline"region and abruptly arrange into a more spheroidal shape (ϵ ≈ 0.7) above the melting point. We attribute the distorted spherical shape above the melting point to thermal fluctuations and intrinsic rigidity of the n-alkyl blocks. We also find evidence for a thin dehydrated PEO layer (≤1 nm) close to the micellar core. The results provide substantial insight into the interplay between crystallinity and molecular packing in confinement and the resulting overall micellar shape.
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| 2. |
- Nielsen, Josefine Eilsø, et al.
(författare)
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Lipid membrane interactions of self-assembling antimicrobial nanofibers : effect of PEGylation
- 2020
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Ingår i: RSC Advances. - : Royal Society of Chemistry. - 2046-2069. ; 10, s. 35329-35340
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Tidskriftsartikel (refereegranskat)abstract
- Supramolecular assembly and PEGylation (attachment of a polyethylene glycol polymer chain) of peptides can be an effective strategy to develop antimicrobial peptides with increased stability, antimicrobial efficacy and hemocompatibility. However, how the self-assembly properties and PEGylation affect their lipid membrane interaction is still an unanswered question. In this work, we use state-of-the-art small angle X-ray and neutron scattering (SAXS/SANS) together with neutron reflectometry (NR) to study the membrane interaction of a series of multidomain peptides, with and without PEGylation, known to self-assemble into nanofibers. Our approach allows us to study both how the structure of the peptide and the membrane are affected by the peptide–lipid interactions. When comparing self-assembled peptides with monomeric peptides that are not able to undergo assembly due to shorter chain length, we found that the nanofibers interact more strongly with the membrane. They were found to insert into the core of the membrane as well as to absorb as intact fibres on the surface. Based on the presented results, PEGylation of the multidomain peptides leads to a slight net decrease in the membrane interaction, while the distribution of the peptide at the interface is similar to the non-PEGylated peptides. Based on the structural information, we showed that nanofibers were partially disrupted upon interaction with phospholipid membranes. This is in contrast with the considerable physical stability of the peptide in solution, which is desirable for an extended in vivo circulation time.
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