Pickering emulsion templated soft capsules by self-assembling cross-linkable ferritin–polymer conjugates

Rijn, Patrick van; Mougin, Nathalie C.; Franke, Daniel; Park, Hyunji; Böker, Alexander

doi:10.1039/c1cc12005k

Cited by 52 publications

(43 citation statements)

References 31 publications

(24 reference statements)

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“…Not only at liquid-liquid interfaces but also onto hydrophobized silicon oxide surfaces [66]. The enhanced assembly at the interface of oil-in-water emulsions resulted in highly stabilized emulsion systems which were transformed into stable protein-polymer capsules by additional cross-linking of the polymer matrix which displayed such a high toughness and flexibility that even anisotropic capsule-networks were formed by intense mixing via extrusion [67,68].…”

Section: Protein Centralized Multiple Polymer Graftsmentioning

confidence: 99%

Polymer Directed Protein Assemblies

Rijn

2013

Polymers

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Protein aggregation and protein self-assembly is an important occurrence in natural systems, and is in some form or other dictated by biopolymers. Very obvious influences of biopolymers on protein assemblies are, e.g., virus particles. Viruses are a multi-protein assembly of which the morphology is dictated by poly-nucleotides namely RNA or DNA. This "biopolymer" directs the proteins and imposes limitations on the structure like the length or diameter of the particle. Not only do these bionanoparticles use polymer-directed self-assembly, also processes like amyloid formation are in a way a result of directed protein assembly by partial unfolded/misfolded biopolymers namely, polypeptides. The combination of proteins and synthetic polymers, inspired by the natural processes, are therefore regarded as a highly promising area of research. Directed protein assembly is versatile with respect to the possible interactions which brings together the protein and polymer, e.g., electrostatic, v.d. Waals forces or covalent conjugation, and possible combinations are numerous due to the large amounts of different polymers and proteins available. The protein-polymer interacting behavior and overall morphology is envisioned to aid in clarifying protein-protein interactions and are thought to entail some interesting new functions and properties which will ultimately lead to novel bio-hybrid materials.

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Section: Protein Centralized Multiple Polymer Graftsmentioning

confidence: 99%

Polymer Directed Protein Assemblies

Rijn

2013

Polymers

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“…66 Ferritin protein cages decorated with poly(N-isopropylacrylamide)/2-(dimethylmaleinimido)-N-ethylacrylamide) (PNIPAM/DMIAAm) were adsorbed at the toluene/water interface.…”

Section: Colloidosome Formation Via Covalent Cross-linkingmentioning

confidence: 99%

Colloidosomes: Synthesis, properties and applications

Thompson

Williams

Armes

2015

Journal of Colloid and Interface Science

197

174

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Colloidosomes represent a rapidly expanding field with various applications in microencapsulation, including the triggered release of cargoes. With self-assembled shells comprising colloidal particles, they offer significant flexibility with respect to microcapsule functionality. This review explores the various types of particles and techniques that have been employed to prepare colloidosomes. The relative advantages and disadvantages of these routes are highlighted and their potential as microcapsules for both small molecule and macromolecular actives is evaluated.

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“…380 Hybrid membranes could be constructed from Pickering emulsions at liquid/liquid as well as liquid/air interfaces by crosslinking the polymer chains. [381][382][383][384] Ferritin acts as a sacrificial template for uniform pores in the polymer membrane that can be created through denaturing the protein (Figure 22b). 384 The permeation through the resulting membrane was controlled by temperature switching below and above the lower critical solution temperature of the polymer.…”

Section: Bionanoparticlesmentioning

confidence: 99%

Surface-initiated controlled radical polymerizations from silica nanoparticles, gold nanocrystals, and bionanoparticles

2015

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In recent years, core/shell nanohybrids containing a nanoparticle core and a distinct surrounding shell of polymer brushes have received extensive attention in nanoelectronics, nanophotonics, catalysis, nanopatterning, drug delivery, biosensing, and many others. From the large variety of existing polymerization methods on the one hand and strategies for grafting onto nanoparticle surfaces on the other hand, the combination of grafting-from with controlled radical polymerization (CRP) techniques has turned out to be the best suited for synthesizing these well-defined core/shell nanohybrids and is known as surface-initiated CRP. Most common among these are surface-initiated atom transfer radical polymerization (ATRP), surface-initiated reversible addition-fragmentation chain transfer (RAFT) polymerization, and surface-initiated nitroxide-mediated polymerization (NMP). This review highlights the state of the art of growing polymers from nanoparticles using surface-initiated CRP techniques. We focus on mechanistic aspects, synthetic procedures, and the formation of complex architectures as well as novel properties. From the vast number of examples of nanoparticle/polymer hybrids formed by surface-initiated CRP techniques, we present nanohybrid formation from the particularly important and most studied silica nanoparticles, gold nanocrystals, and proteins which can be regarded as bionanoparticles

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Pickering emulsion templated soft capsules by self-assembling cross-linkable ferritin–polymer conjugates

Cited by 52 publications

References 31 publications

Polymer Directed Protein Assemblies

Polymer Directed Protein Assemblies

Colloidosomes: Synthesis, properties and applications

Surface-initiated controlled radical polymerizations from silica nanoparticles, gold nanocrystals, and bionanoparticles

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