Dataset Information

Permeable Protein-Loaded Polymersome Cascade Nanoreactors by Polymerization-Induced Self-Assembly.

ABSTRACT: Enzyme loading of polymersomes requires permeability to enable them to interact with the external environment, typically requiring addition of complex functionality to enable porosity. Herein, we describe a synthetic route towards intrinsically permeable polymersomes loaded with functional proteins using initiator-free visible light-mediated polymerization-induced self-assembly (photo-PISA) under mild, aqueous conditions using a commercial monomer. Compartmentalization and retention of protein functionality was demonstrated using green fluorescent protein as a macro-molecular chromophore. Catalytic enzyme-loaded vesicles using horseradish peroxidase and glucose oxidase were also prepared and the permeability of the membrane towards their small molecule substrates was revealed for the first time. Finally, the interaction of the compartmentalized enzymes between separate vesicles was validated by means of an enzymatic cascade reaction. These findings have a broad scope as the methodology could be applied for the encapsulation of a large range of macromolecules for advancements in the fields of nanotechnology, biomimicry and nanomedicine.

SUBMITTER: Blackman LD

PROVIDER: S-EPMC5718297 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature

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Permeable Protein-Loaded Polymersome Cascade Nanoreactors by Polymerization-Induced Self-Assembly.

Blackman Lewis D LD Varlas Spyridon S Arno Maria C MC Fayter Alice A Gibson Matthew I MI O'Reilly Rachel K RK

ACS macro letters 20171001 11

Enzyme loading of polymersomes requires permeability to enable them to interact with the external environment, typically requiring addition of complex functionality to enable porosity. Herein, we describe a synthetic route towards intrinsically permeable polymersomes loaded with functional proteins using initiator-free visible light-mediated polymerization-induced self-assembly (photo-PISA) under mild, aqueous conditions using a commercial monomer. Compartmentalization and retention of protein f ...[more]

PMID: 29226025

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Project description:The dynamic interactions of membranes, particularly their fusion and fission, are critical for the transmission of chemical information between cells. Fusion is primarily driven by membrane tension built up through membrane deformation. For artificial polymersomes, fusion is commonly induced via the external application of a force field. Herein, fusion-promoted development of anisotropic tubular polymersomes (tubesomes) was achieved in the absence of an external force by exploiting the unique features of aqueous ring-opening metathesis polymerization-induced self-assembly (ROMPISA). The out-of-equilibrium tubesome morphology was found to arise spontaneously during polymerization, and the composition of each tubesome sample (purity and length distribution) could be manipulated simply by targeting different core-block degrees of polymerization (DPs). The evolution of tubesomes was shown to occur via fusion of "monomeric" spherical polymersomes, evidenced most notably by a step-growth-like relationship between the fraction of tubular to spherical nano-objects and the average number of fused particles per tubesome (analogous to monomer conversion and DP, respectively). Fusion was also confirmed by Förster resonance energy transfer (FRET) studies to show membrane blending and confocal microscopy imaging to show mixing of the polymersome lumens. We term this unique phenomenon polymerization-induced polymersome fusion, which operates via the buildup of membrane tension exerted by the growing polymer chains. Given the growing body of evidence demonstrating the importance of nanoparticle shape on biological activity, our methodology provides a facile route to reproducibly obtain samples containing mixtures of spherical and tubular polymersomes, or pure samples of tubesomes, of programmed length. Moreover, the capability to mix the interior aqueous compartments of polymersomes during polymerization-induced fusion also presents opportunities for its application in catalysis, small molecule trafficking, and drug delivery.

Dataset Information

Permeable Protein-Loaded Polymersome Cascade Nanoreactors by Polymerization-Induced Self-Assembly.

Publications

Permeable Protein-Loaded Polymersome Cascade Nanoreactors by Polymerization-Induced Self-Assembly.

Similar Datasets

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