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

DOI: 10.1021/acsabm.9b00489 DOI Help

Authors: Valeria Castelletto (University of Reading) , Charlotte J. C. Edwards-gayle (University of Reading) , Ian W. Hamley (Diamond Light Source) , Juliane N. B. D. Pelin (Centro de Ciências Naturais e Humanas) , Wendel Andrade Alves (Centro de Ciências Naturais e Humanas) , Andrea Aguilar (Instituto de Ciências Ambientais, Químicas e Farmacêuticas, Universidade Federal de São) , Jani Seitsonen (Aalto University) , Janne Ruokolainen (Aalto University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acs Applied Bio Materials

State: Published (Approved)
Published: July 2019
Diamond Proposal Number(s): 21470

Open Access Open Access

Abstract: 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.

Journal Keywords: Lipopeptides; Peptide Amphiphiles; Self-Assembly; Micelles; Cubosomes; Catalysis; Aldol reaction

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: B21-High Throughput SAXS

Other Facilities: ESRF