Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/9621
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dc.contributor.authorAlshanski, Israelen_US
dc.contributor.authorTORASKAR, SURAJen_US
dc.contributor.authorGordon-Levitan, Danielen_US
dc.contributor.authorMassetti, Marcoen_US
dc.contributor.authorJAIN, PRASHANTen_US
dc.contributor.authorVaccaro, Luigien_US
dc.contributor.authorKIKKERI, RAGHAVENDRAen_US
dc.contributor.authorHurevich, Mattanen_US
dc.contributor.authorYitzchaik, Shlomoen_US
dc.date.accessioned2025-04-15T07:00:08Z-
dc.date.available2025-04-15T07:00:08Z-
dc.date.issued2024-04en_US
dc.identifier.citationLangmuir, 40(14),7471–7478.en_US
dc.identifier.urihttps://doi.org/10.1021/acs.langmuir.3c03943en_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/9621-
dc.description.abstractNeuraminidases (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.en_US
dc.language.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.subjectChromatographyen_US
dc.subjectElectrodesen_US
dc.subjectLayersen_US
dc.subjectPeptides and proteinsen_US
dc.subjectSurface interactionsen_US
dc.subject2024en_US
dc.titleSurface-Controlled Sialoside-Based Biosensing of Viral and Bacterial Neuraminidasesen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Chemistryen_US
dc.identifier.sourcetitleLangmuiren_US
dc.publication.originofpublisherForeignen_US
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