ArticleLangmuir : the ACS journal of surfaces and colloids2024
Surface-Controlled Sialoside-Based Biosensing of Viral and Bacterial Neuraminidases.
Article in Langmuir : the ACS journal of surfaces and colloids, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Research Progress and Screening Strategies of Natural Product-Derived Neuraminidase Inhibitors.Biosensors · 2026Review
- Metal-Mediated Il-8 Binding to Heparan Sulfate Evaluated by Electrochemical Impedance Spectroscopy.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Impedimetric Characterization of NanA Structural Domains Activity on Sialoside-Containing Interfaces.Langmuir : the ACS journal of surfaces and colloids · 2024Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neuraminidases (NA) are sialic acid-cleaving enzymes that are used by both bacteria and viruses. These enzymes have sialoside structure-related binding and cleaving preferences. Differentiating between these enzymes requires using a large array of hard-to-access sialosides. In this work, we used electrochemical impedimetric biosensing to differentiate among several pathogene-related NAs. We used a limited set of sialosides and tailored the surface properties. Various sialosides were grafted on two different surfaces with unique properties. Electrografting on glassy carbon electrodes provided low-density sialoside-functionalized surfaces with a hydrophobic submonolayer. A two-step assembly on gold electrodes provided a denser sialoside layer on a negatively charged submonolayer. The synthesis of each sialoside required dozens of laborious steps. Utilizing the unique protein-electrode interaction modes resulted in richer biodata without increasing the synthetic load. These principles allowed for profiling NAs and determining the efficacy of various antiviral inhibitors.
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