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Self-assembly of a catalytically active lipopeptide and its incorporation into cubosomes

Castelletto, V., Edwards-Gayle, C., Hamley, I. W., Pelin, J., Alves, W. A., Aguilar, A., Seitsonen, J. and Ruokolainen, J. (2019) Self-assembly of a catalytically active lipopeptide and its incorporation into cubosomes. ACS Applied Bio Materials, 2 (8). pp. 3639-3647. ISSN 2576-6422

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To link to this item DOI: 10.1021/acsabm.9b00489


The self-assembly and biocatalytic activity of the proline-functionalized lipopeptide PRW-NH-C16 are examined, and compared to that of the related PRW-O-C16 lipopeptide, which differs in having an ester linker between the lipid chain and tripeptide headgroup instead of an amide linker. Lipopeptide PRW-NH-C16 self-assembles into spherical micelles above a critical aggregation concentration, similar to the behaviour of PRW-O-C16 reported previously [B.M. Soares et al. Phys. Chem. Chem. Phys., 2017, 19, 1181—1189]. However, PRW-NH-C16 shows improved catalytic activity in a model aldol reaction. In addition, we explore incorporation of the biocatalytic lipopeptide into lipid cubosomes. SAXS shows that increasing lipopeptide concentration leads to an expansion of the monoolein cubosome lattice spacing, and loss of long-range cubic order as the lipopeptide is encapsulated in the cubosomes. At higher loadings of lipopeptide, reduced cubosome formation is observed at the expense of vesicle formation. Our results show that the peptide-lipid chain linker does not influence self-assembly but does impart improved biocatalytic activity. Furthermore, we show that lipopeptides can be incorporated into lipid cubosomes, leading to restructuring into vesicles at high loadings. These findings point the way towards the future development of bioactive lipopeptide assemblies and slow release cubosome-based delivery systems.

Item Type:Article
Divisions:Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:84906
Publisher:American Chemical Society (ACS)


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