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dc.contributor.authorC. Wilson, Jenniferen_US
dc.contributor.authorJ. Thomson, Robinen_US
dc.contributor.authorC. Dyason, Jeffreyen_US
dc.contributor.authorFlorio, Pasen_US
dc.contributor.authorJ. Quelch, Kayleneen_US
dc.contributor.authorAbo, Samiaen_US
dc.contributor.authorvon Itzstein, Marken_US
dc.date.accessioned2017-04-24T09:17:08Z
dc.date.available2017-04-24T09:17:08Z
dc.date.issued2000en_US
dc.date.modified2014-07-21T05:06:46Z
dc.identifier.issn09574166en_US
dc.identifier.doi10.1016/S0957-4166(99)00552-2en_US
dc.identifier.urihttp://hdl.handle.net/10072/22207
dc.description.abstractA molecular modelling study using the program GRID has been used to investigate the structural requirements of a potential inhibitor binding to Vibrio cholerae sialidase. A number of favourable interactions were predicted between the sialidase and Neu2en derivatives containing hydroxyl- or halogen-substituted acyl groups on the C-5 amine. As a result of this study, a detailed analysis of the interactions of C-5-substituted Neu2en derivatives with the active site of V. cholerae sialidase was undertaken using a conformational searching routine based on molecular dynamics. Based on the results of these molecular design studies several N-acyl-Neu2en-based probes were prepared and evaluated for sialidase inhibition. As envisaged, and pleasingly, the designed compounds were found to be accommodated by the enzyme's active site architecture, and to be strong inhibitors of V. cholerae sialidase.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_US
dc.languageEnglishen_US
dc.language.isoen_US
dc.publisherPergamonen_US
dc.publisher.placeUnited Kingdomen_US
dc.relation.ispartofpagefrom53en_US
dc.relation.ispartofpageto73en_US
dc.relation.ispartofissue1en_US
dc.relation.ispartofjournalTetrahedron Asymmetryen_US
dc.relation.ispartofvolume11en_US
dc.subject.fieldofresearchHISTORY AND ARCHAEOLOGYen_US
dc.subject.fieldofresearchcode210000en_US
dc.titleThe design, synthesis and biological evaluation of neuraminic acid-based probes of Vibrio cholerae sialidaseen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2000
gro.hasfulltextNo Full Text


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