Nowadays, intelligent vehicles are equipped with a number of advanced sensors, such as radar and cameras [...].
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| http://dx.doi.org/10.3390/s23167015 | DOI Listing |
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Evaluation of synaptotagmin-1 action models by all-atom molecular dynamics simulations.
FEBS Open Bio
January 2025
Institute of Neurophysiology, Charité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Germany.
Neurotransmitter release is triggered in microseconds by the two C domains of the Ca sensor synaptotagmin-1 and by SNARE complexes, which form four-helix bundles that bridge the vesicle and plasma membranes. The synaptotagmin-1 CB domain binds to the SNARE complex via a 'primary interface', but the mechanism that couples Ca-sensing to membrane fusion is unknown. Widespread models postulate that the synaptotagmin-1 Ca-binding loops accelerate membrane fusion by inducing membrane curvature, perturbing lipid bilayers or helping bridge the membranes, but these models do not seem compatible with SNARE binding through the primary interface, which orients the Ca-binding loops away from the fusion site.
View Article and Find Full Text PDFDeep learning empowered sensor fusion boosts infant movement classification.
Commun Med (Lond)
January 2025
Child and Adolescent Psychiatry and Psychotherapy, University Medical Center Göttingen, Leibniz ScienceCampus Primate Cognition and German Center for Child and Adolescent Health (DZKJ), Göttingen, Germany.
Background: To assess the integrity of the developing nervous system, the Prechtl general movement assessment (GMA) is recognized for its clinical value in diagnosing neurological impairments in early infancy. GMA has been increasingly augmented through machine learning approaches intending to scale-up its application, circumvent costs in the training of human assessors and further standardize classification of spontaneous motor patterns. Available deep learning tools, all of which are based on single sensor modalities, are however still considerably inferior to that of well-trained human assessors.
View Article and Find Full Text PDFFluorescence Anisotropy for Monitoring cis- and trans-Membrane Interactions of Synaptotagmin-1.
Methods Mol Biol
January 2025
Neurological Disorders Research Center, Qatar Biomedical Research Institute (QBRI), Hamad Bin Khalifa University (HBKU), Qatar Foundation, Doha, Qatar.
Vesicle fusion induces neurotransmitter release, orchestrated by synaptotagmin-1 (Syt-1) as a Ca sensor. However, the precise molecular mechanisms of Syt-1 remain controversial, with various and competing models proposed based on different ionic strengths. Syt-1, residing on the vesicle membrane alongside anionic phospholipids such as phosphatidylserine (PS), undergoes Ca-induced binding to its own vesicle membrane, known as the cis-interaction, which prevents the trans-interaction of Syt-1 with the plasma membrane.
View Article and Find Full Text PDFMolecular Dynamics Simulations of the SNARE Complex Interacting with Synaptotagmin, Complexin, and Lipid Bilayers.
Methods Mol Biol
January 2025
Departments of Neurology, and Anatomy and Cell Biology, Wayne State University School of Medicine, University Health Center, Detroit, MI, USA.
Molecular dynamics (MD) simulations enable in silico investigation of the dynamic behavior of proteins and protein complexes. Here, we describe MD simulations of the SNARE bundle forming the complex with the neuronal proteins Synaptotagmin-1 (Syt1) and Complexin (Cpx). Syt1 is the synaptic vesicle (SV) protein that serves as the neuronal calcium sensor and triggers synaptic fusion upon calcium binding, and this process is promoted and accelerated by Cpx.
View Article and Find Full Text PDFMonitoring of enzymatic cleavage reaction of GST-fusion protein on biolayer interferometry sensor.
Biophys Physicobiol
September 2024
Faculty of Pharmaceutical Sciences, Hokkaido University of Science, Sapporo, Hokkaido 006-8585, Japan.
Biolayer interferometry (BLI) is an optical sensor-based analytical method primarily used for analyzing interactions between biomolecules. In this study, we explored the application of BLI to observe the cleavage reaction of glutathione S-transferase (GST)-tagged fusion protein by human rhinovirus (HRV) 3C protease on a BLI sensor as a new application of the BLI method. The soluble domain of the Tic22 protein from was expressed and purified as a GST-tagged fusion protein, GST-Tic22, in .
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