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Tuning the bioactivity of tensioactive deoxy glycosides to structure: antibacterial activity versus selective cholinesterase inhibition rationalized by molecular docking

2013Journal article Open access
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authorProfile.affiliationInstituto Politécnico de Santarém_Escola Superior Agráriapt_PT
dc.contributor.authorMartins, A.
dc.contributor.authorSantos, M.S.
dc.contributor.authorDias, C.
dc.contributor.authorSerra, P.
dc.contributor.authorCachatra, V.
dc.contributor.authorPais, J.
dc.contributor.authorCaio, J.
dc.contributor.authorTeixeira, V.H.
dc.contributor.authorMachuqueiro, M.
dc.contributor.authorSilva, M.S.
dc.contributor.authorPelerito, A.
dc.contributor.authorJustino, Jorge
dc.contributor.authorGoulart, Margarida
dc.contributor.authorSilva, Filipa
dc.contributor.authorRauter, A.P.
dc.date.accessioned2023-03-24T15:01:01Z
dc.date.available2023-03-24T15:01:01Z
dc.date.issued2013
dc.description.abstractNew octyl/dodecyl 2,6-dideoxy-D-arabino-hexopyranosides have been synthesized by a simple but efficient methodology based on the reaction of glycals with alcohols catalysed by triphenylphosphane hydrobromide, deprotection, regioselective tosylation and reduction. Their surface-active properties were evaluated in terms of adsorption and aggregation parameters and compared with those of 2-deoxy-D-glycosides and 2,6-dideoxy-L-glycosides. Deoxygenation at the 6-position led to a decrease in the critical micelle concentration, and an increase in the adsorption efficiency (pC20) promoting aggregation more efficiently than adsorption. With regard to the antibacterial activity, dodecyl 2,6-dideoxy-α-L-arabino-hexopyranoside was the most active compound towards Bacillus anthracis (MIC 25 μM), whereas its enantiomer exhibited a MIC value of 50 μM. Both 2,6-dideoxy glycosides were active towards Bacillus cereus, Bacillus subtilis, Enterococcus faecalis and Listeria monocytogenes. In contrast, none of the 2-deoxy glycosides was significantly active. These results and the data on surface activity suggest that aggregation is a key issue for antimicrobial activity. Beyond infection, Alzheimer’s disease also threatens elderly populations. In the search for butyrylcholinesterase (BChE) selective inhibition, 2- deoxy glycosides were screened in vitro by using Ellman’s assay. Octyl 2-deoxy-α-D-glycoside was found to be a BChE selective inhibitor promoting competitive inhibition. Docking studies supported these results as they pinpoint the importance of the primary OH group in stabilizing the BChE inhibitor complex. A size-exclusion mechanism for inhibition has been proposed based on the fact that acetylcholinesterase (AChE) exhibits several bulky residues that hinder access to the active-site cavity. This work shows how the deoxygenation pattern, configuration and functionality of the anomeric centre can tune physical and surface properties as well as the bioactivity of these multifunctional and stereochemically rich molecules.pt_PT
dc.description.sponsorshipFEDER e FCTpt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationMartins, A.; Santos, M.S.; Dias, C.; Serra, P.; Cachatra, V.; Pais, J.; Caio, J.; Teixeira, V.H.; Machuqueiro, M.; Silva, M.S.; Pelerito, A.; Justino, J.; Goulart, M.; Silva, F.V. and Rauter, A.P. (2013), Tuning the bioactivity of tensioactive deoxy glycosides to structure: antibacterial activity versus selective cholinesterase inhibition rationalized by molecular docking. European Journal of Organic Chemistry, 2013, 1448-1459. https://doi.org/10.1002/ejoc.201201520pt_PT
dc.identifier.doihttps://doi.org/10.1002/ejoc.201201520pt_PT
dc.identifier.eissn1099-0690
dc.identifier.urihttp://hdl.handle.net/10400.15/4370
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherWileypt_PT
dc.relationIncentive System – Research & Technological Development Co-Promotion Project nr. 21457 - FEDERpt_PT
dc.relationPost-doctoral research grant BPD/42567/2007 - FCTpt_PT
dc.relationCQB Strategic Project PEst-OE/QUI/UI0612/2011 - FCTpt_PT
dc.relation.publisherversionhttps://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/ejoc.201201520pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectSynthetic methodspt_PT
dc.subjectMedicinal chemistrypt_PT
dc.subjectGlycosidespt_PT
dc.subjectSurfactantspt_PT
dc.subjectBiological activitypt_PT
dc.subjectMolecular dockingpt_PT
dc.subjectMétodos de síntesept_PT
dc.subjectAplicação em medicinapt_PT
dc.subjectGlicosídeospt_PT
dc.subjectSurfactantespt_PT
dc.subjectActividade biológicapt_PT
dc.subjectAncoragem molecularpt_PT
dc.titleTuning the bioactivity of tensioactive deoxy glycosides to structure: antibacterial activity versus selective cholinesterase inhibition rationalized by molecular dockingpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.conferencePlaceWeinheimpt_PT
oaire.citation.endPage1459pt_PT
oaire.citation.startPage1448pt_PT
oaire.citation.titleEuropean Journal of Organic Chemistrypt_PT
oaire.citation.volume2013pt_PT
person.familyNameJustino
person.familyNameVinagre Marques da Silva
person.givenNameJorge
person.givenNameFilipa
person.identifierhttps://scholar.google.pt/citations?hl=pt-PT&user=TcUz9ZAAAAAJ
person.identifier.ciencia-idB610-66DA-A3AC
person.identifier.orcid0000-0003-3114-5926
person.identifier.orcid0000-0003-4700-2938
person.identifier.scopus-author-id22942414000
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication3e483773-36b8-4a7b-82f3-c0a39f6a7fa9
relation.isAuthorOfPublication344bf736-31c9-4a35-844c-67a176174a44
relation.isAuthorOfPublication.latestForDiscovery344bf736-31c9-4a35-844c-67a176174a44

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