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dc.contributor.authorCarroux, Cindy J
dc.contributor.authorRankin, Gregory M
dc.contributor.authorMoeker, Janina
dc.contributor.authorBornaghi, Laurent F
dc.contributor.authorKatneni, Kasiram
dc.contributor.authorMorizzi, Julia
dc.contributor.authorCharman, Susan A
dc.contributor.authorVullo, Daniela
dc.contributor.authorSupuran, Claudiu T
dc.contributor.authorPoulsen, Sally-Ann
dc.date.accessioned2017-05-03T11:45:44Z
dc.date.available2017-05-03T11:45:44Z
dc.date.issued2013
dc.identifier.issn0022-2623
dc.identifier.doi10.1021/jm401163e
dc.identifier.urihttp://hdl.handle.net/10072/57021
dc.description.abstractThe selective inhibition of cancer-associated human carbonic anhydrase (CA) enzymes, specifically CA IX and XII, has been validated as a mechanistically novel approach toward personalized cancer management. Herein we report the design and synthesis of a panel of 24 novel glycoconjugate primary sulfonamides that bind to the extracellular catalytic domain of CA IX and XII. These compounds were synthesized from variably acylated glycopyranosyl azides and either 3- or 4-ethynyl benzene sulfonamide using Cu(I)-catalyzed azide alkyne cycloaddition (CuAAC). The CA enzyme inhibition profile for all compounds was determined, while in vitro metabolic stability, plasma stability, and plasma protein binding for a representative set of compounds was measured. Our findings demonstrate the influence of the differing acyl groups on these key biopharmaceutical properties, confirming that acyl group protected carbohydrate-based sulfonamides have potential as prodrugs for selectively targeting the extracellular cancer-associated CA enzymes.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent400838 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherAmerican Chemical Society
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationY
dc.relation.ispartofpagefrom9623
dc.relation.ispartofpageto9634
dc.relation.ispartofissue23
dc.relation.ispartofjournalJournal of Medicinal Chemistry
dc.relation.ispartofvolume56
dc.rights.retentionY
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchBiologically active molecules
dc.subject.fieldofresearchOrganic chemistry
dc.subject.fieldofresearchPharmacology and pharmaceutical sciences
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode340401
dc.subject.fieldofresearchcode3405
dc.subject.fieldofresearchcode3214
dc.titleA prodrug approach toward cancer-related carbonic anhydrase inhibition
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.facultyGriffith Sciences, Griffith Institute for Drug Discovery
gro.rights.copyrightThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Medicinal Chemistry, copyright 2012 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/jm401163e.
gro.date.issued2015-07-30T23:12:48Z
gro.hasfulltextFull Text
gro.griffith.authorPoulsen, Sally-Ann


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