2017, Sykora, Sabine, Correro, Maria Rita, Moridi, Negar, Belliot, Gaël, Pothier, Pierre, Dudal, Yves, Corvini, Philippe, Shahgaldian, Patrick

The design of nanomaterials that are capable of specific and sensitive biomolecular recognition is an on-going challenge in the chemical and biochemical sciences. A number of sophisticated artificial systems have been designed to specifically recognize a variety of targets. However, methods based on natural biomolecular detection systems using antibodies are often superior. Besides greater affinity and selectivity, antibodies can be easily coupled to enzymatic systems that act as signal amplifiers, thus permitting impressively low detection limits. The possibility to translate this concept to artificial recognition systems remains limited due to design incompatibilities. Here we describe the synthesis of a synthetic nanomaterial capable of specific biomolecular detection by using an internal biocatalytic colorimetric detection and amplification system. The design of this nanomaterial relies on the ability to accurately grow hybrid protein-organosilica layers at the surface of silica nanoparticles. The method allows for label-free detection and quantification of targets at picomolar concentrations.

2015-01-05, Sykora, Sabine, Belliot, Gaël, Pothier, Pierre, Cumbo, Alessandro, Arnal, Charlotte, Dudal, Yves, Corvini, Philippe, Shahgaldian, Patrick

Functional recognition imprints of virus-like particles, at the surface of silica particles, were generated following a strategy based on protein-templated polycondensation of organosilanes.

2016, Correro, Maria Rita, Moridi, Negar, Schützinger, Hansjörg, Sykora, Sabine, Ammann, Erik, Peters, E. Henrik, Dudal, Yves, Corvini, Philippe, Shahgaldian, Patrick

The fragile nature of most enzymes is a major hindrance to their use in industrial processes. Herein, we describe a synthetic chem. strategy to produce hybrid org.​/inorg. nanobiocatalysts; it exploits the self-​assembly of silane building blocks at the surface of enzymes to grow an organosilica layer, of controlled thickness, that fully shields the enzyme. Remarkably, the enzyme triggers a rearrangement of this organosilica layer into a significantly soft structure. We demonstrate that this change in stiffness correlates with the biocatalytic turnover rate, and that the organosilica layer shields the enzyme in a soft environment with a markedly enhanced resistance to denaturing stresses.

2015-12-15, Xiao, Pu, Weibel, Nicolas, Dudal, Yves, Corvini, Philippe, Shahgaldian, Patrick