Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/9472
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dc.contributor.authorANAND, SAURABHen_US
dc.contributor.authorMARDHEKAR, SANDHYAen_US
dc.contributor.authorBHOGE, PREETI RAVINDRAen_US
dc.contributor.authorMISHRA, SANDEEP KUMARen_US
dc.contributor.authorKIKKERI, RAGHAVENDRAen_US
dc.date.accessioned2025-04-15T06:48:29Z-
dc.date.available2025-04-15T06:48:29Z-
dc.date.issued2024-04en_US
dc.identifier.citationChemical Communications, 60(33), 4495-4498.en_US
dc.identifier.issn1359-7345en_US
dc.identifier.issn1364-548Xen_US
dc.identifier.urihttps://doi.org/10.1039/D4CC00464Gen_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/9472-
dc.description.abstractWe have demonstrated that cisplatin (CP), an anticancer drug, showed a preference for binding the sulfated-L-iduronic acid (S-L-IdoA) unit over the sulfated-D-glucuronic acid unit of heparan sulfate. The multivalency of S-L-IdoA, such as in the proteoglycan mimic, resulted in distinct modes of cell-surface engineering in normal and cancer cells, with these disparities having a significant impact on CP-mediated toxicity.en_US
dc.language.isoenen_US
dc.publisherRoyal Society of Chemistryen_US
dc.subjectChemistryen_US
dc.subject2024en_US
dc.titleMolecular recognition and proteoglycan mimic arrangement: modulating cisplatin toxicityen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Chemistryen_US
dc.identifier.sourcetitleChemical Communicationsen_US
dc.publication.originofpublisherForeignen_US
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