Biomimetic and biopolymer-based enzyme encapsulation.

Encapsulated enzymes are stable under various conditions and used in enzyme therapy, catalysis, and biosensors. The capsules are often inspired by structures from nature such as viral capsids, DNA motifs and diatom frustules. They are based on inorganic minerals as well as soft or polymeric materials, or even a combination of these.

Biomimetic Silica Encapsulation of Lipid Nanodiscs and β-Sheet-Stabilized Diacylglycerol Kinase.

Integral membrane proteins (IMPs) comprise highly important classes of proteins such as transporters, sensors, and channels, but their investigation and biotechnological application are complicated by the difficulty to stabilize them in solution. We set out to develop a biomimetic procedure to encapsulate functional integral membrane proteins in silica to facilitate their handling under otherwise detrimental conditions and thereby extend their applicability. To this end, we designed and expressed new fusion constructs of the membrane scaffold protein MSP with silica-precipitating peptides based on the R5 sequence from the diatom .

Continuous Flow Reactors from Microfluidic Compartmentalization of Enzymes within Inorganic Microparticles.

Compartmentalization and selective transport of molecular species are key aspects of chemical transformations inside the cell. In an artificial setting, the immobilization of a wide range of enzymes onto surfaces is commonly used for controlling their functionality but such approaches can restrict their efficacy and expose them to degrading environmental conditions, thus reducing their activity. Here, we employ an approach based on droplet microfluidics to generate enzyme-containing microparticles that feature an inorganic silica shell that forms a semipermeable barrier.

Silica particles with a quercetin-R5 peptide conjugate are taken up into HT-29 cells and translocate into the nucleus.

Intracellular delivery of bioactive polyphenols is currently evaluated as a protective strategy for cells under pharmaceutical stress. To this end, the 20mer R5 peptide from the marine diatom C. fusiformis was N-terminally modified with a quercetin derivative.