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Intramolecular trigger remodeling-induced HCR for amplified detection of protein-specific glycosylation.
- Source :
-
Talanta [Talanta] 2020 Aug 01; Vol. 215, pp. 120889. Date of Electronic Publication: 2020 Mar 07. - Publication Year :
- 2020
-
Abstract
- Dynamic changes of protein-glycosylation on cell surface act as an important indicator that reflects cellular physiological states and disease developments. The enhanced visualization of protein-specific glycosylation is of great value to interpret its functions and mechanisms. Hence, we present an intramolecular trigger remodeling-induced hybridization chain reaction (HCR) for imaging protein-specific glycosylation. This strategy relies on designing two DNA probes, protein and glycan probes, labeled respectively on protein by aptamer recognition and glycan through metabolic oligosaccharide engineering (MOE). Upon the same glycoprotein was labeled, the complementary domain of two probes induces hybridization and thus to remodel an intact trigger, followed by initiating HCR assembly. Applying this strategy, we successfully achieved imaging of specific protein-glycosylation on CEM cell surface and monitored dynamic changes of the glycosylation after treating with drugs. It provides a powerful tool with high flexibility, specificity and sensitivity in the research field of protein-specific glycosylation on living cells.<br />Competing Interests: Declaration of competing interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2020 Elsevier B.V. All rights reserved.)
- Subjects :
- Aptamers, Nucleotide chemistry
Cell Adhesion Molecules antagonists & inhibitors
Cell Adhesion Molecules metabolism
Cells, Cultured
DNA Probes chemical synthesis
Glycosylation drug effects
Humans
Particle Size
Polysaccharides analysis
Receptor Protein-Tyrosine Kinases antagonists & inhibitors
Receptor Protein-Tyrosine Kinases metabolism
Surface Properties
Tunicamycin pharmacology
Cell Adhesion Molecules analysis
DNA Probes chemistry
Nucleic Acid Hybridization
Receptor Protein-Tyrosine Kinases analysis
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3573
- Volume :
- 215
- Database :
- MEDLINE
- Journal :
- Talanta
- Publication Type :
- Academic Journal
- Accession number :
- 32312435
- Full Text :
- https://doi.org/10.1016/j.talanta.2020.120889