Search bioRxiv⌕ Search

Biology subjects

Desgarceaux, R.

Publications and source records attributed to Desgarceaux, R..

2 recordsLinked to original sources

Wafer-scale integration of alpha-quartz thin films towards super high frequency piezoelectric bioNEMS for arbovirus detection

Micro and nanoelectromechanical systems (MEMS/NEMS), especially piezoelectric resonators, offer a promising strategy for the manufacturing of point-of-care devices providing rapid, sensitive, and field-deployable tests with minimal user training for the diagnostic of viral infections. High-frequency (HF) MEMS/NEMS have the potential for ultrasensible mass-loading devices. Yet, their use for biomedical applications requires challenging manufacturing qualities. Here, we develop a large-scale chemical integration of epitaxial -quartz (100) thin films on silicon wafers up to 4-inches. This methodology allows the microfabrication of wafer-scale piezoelectric -quartz/silicon bioMEMS using a recognition layer capable of selectively detecting emerging arboviruses over other viral loads. Using contact-free vibrometry, we show a mass sensitivity of the bioMEMS device of 22.4 pg/Hz in liquid conditions and a Chikungunya virus limit of detection of 9 ng/ml. To reach piezoelectric transduction for compact quartz sensor devices, we develop NEMS resonators at super HF, i.e., 17.8 GHz with a quality factor of 280 which represents a QxF product of 4.98{middle dot}1012. These -quartz NEMS can reach thicknesses between 100 and 800 nm and lateral dimensions up to 9 mm2. Our work opens the door for cost-efficient single-chip epitaxial piezoelectric -quartz/Si ultrasensitive NEMS sensors manufactured exclusively by soft-chemistry for biomedical applications and many other fields.

bioengineering↗

Septin filament assembly assists the lateral organization of membranes

Compartmentalized interactions of plasma membrane components are essential to support many cell functions, from signaling to cell division, adhesion, migration, or phagocytosis. Cytoskeletal-membrane interactions play an important role in forming membrane compartments, and this feature has been primarily studied through the actin cytoskeleton. Unlike actin, septins directly interact with membranes, acting as scaffolds to recruit proteins to specific cellular locations and as structural diffusion barriers for membrane components. However, how septins interact with and remodel the local membrane environment is unclear. Here we combined minimal reconstituted systems based on fluorescence microscopy and quantitative atomic force microscopy together with live yeast cell imaging and STED microscopy to study septin-mediated membrane organization. Our results show that septins self-assembly into filament-based sub-micrometric patches and high-order structures prompt their membrane-organizing role in vitro and in yeast cells, respectively. Furthermore, we show that the polybasic domain of Cdc11, in addition to the amphipathic helix of Cdc12, plays an essential role in supporting the membrane remodeling and curvature-sensing properties of yeast septins. Collectively, our work provides a framework for understanding the molecular mechanisms by which septins can support cellular functions intimately linked to membranes.

cell biology↗