A functionally tunable magnetic nanochains platform for N-glycoproteomic analysis of extracellular vesicles from ultratrace biofluids.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 40819088.
- Also identified by DOI 10.1038/s41467-025-63075-0 and PMC identifier 12357864.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
Extracellular vesicles (EVs) carry complex glycoproteins critical mediators of disease progression and hold great potential for liquid biopsy applications. However, their low abundance presents significant analytical challenges. This study develop a versatile platform for EV N-glycoproteomic analysis (EVGpro), which enables tandem EV capture, EV protein digestion, and enrichment of N-glycopeptides. Functionalized magnetic nanochains with cell-penetrating peptides (octa-arginine, R<sub>8</sub>) enable efficient EV isolation, followed by on-chain hydrolysis to expose PEG<sub>2000</sub> for ultrasensitive glycopeptide enrichment. The streamlined EVGpro platform identified up to 17 times more EV glycoproteins than ultracentrifugation across seven biofluids, profiling 398 EV glycoproteins from just 1 μL tear. Applied to seminal plasma, EVGpro uncover disease-specific glycoprotein signatures and identified previously unreported subtypes of asthenozoospermia. This robust and scalable approach advances the sensitive detection of disease biomarkers and molecular subtypes from diverse biofluids to enable precision medicine.
Medical subject headings
- Extracellular Vesicles
- Proteomics
- Glycoproteins
- Body Fluids