Topic: proximity-dependent biotinylation

The application of biotin ligase or peroxidase fused with specific proteins or subcellular regions, combined with mass spectrometry-based quantitative proteomics, has become a potent approach for unravelling molecular interactions and determining the locations of native proteins based on their proximity. Recent applications of proximity-dependent biotinylation in neuroscience have yielded insights into the composition of sub-synaptic structures, including the synaptic cleft [1].Despite the effectiveness of proximity labelling methods in providing a global perspective on protein-protein interac

This study aims to investigate the small extracellular vesicle (sEV) impact on the blood-brain barrier (BBB), particularly the interactions between sEVs and brain endothelial cells (BECs). The molecular components governing these interactions are currently unknown. In order to identify sEV-BEC interactors, a novel assay based on proximity-dependent biotinylation was developed. sEVs purified from a panel of cell lines derived from various peripheral and brain-derived tumors, including HEK293 embryonic kidney cells, SK-MEL-28 skin melanoma, A549 lung adenocarcinoma, MDA-MB-231 breast adenocarcin