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dc.contributor.authorBonache de Marcos, María Ángeles-
dc.contributor.authorAlaimo, Alessandro-
dc.contributor.authorMalo, Covadonga-
dc.contributor.authorMillet, Oscar-
dc.contributor.authorVillarroel, Alvaro-
dc.contributor.authorGonzález-Muñiz, Rosario-
dc.date.accessioned2014-11-25T12:12:41Z-
dc.date.available2014-11-25T12:12:41Z-
dc.date.issued2014-
dc.identifierdoi: 10.1039/c4ob01338g-
dc.identifierissn: 1477-0520-
dc.identifiere-issn: 1477-0539)-
dc.identifier.citationOrganic and Biomolecular Chemistry 12: 8877- 8887 (2014)-
dc.identifier.urihttp://hdl.handle.net/10261/108026-
dc.description.abstractThe recombinant Kv7.2 calmodulin (CaM) binding site (Q2AB CaMBD) shows a high tendency to aggregate, thus complicating biochemical and structural studies. To facilitate these studies we have conceived bis-PEG-peptide CaMBD-mimetics linking helices A and B in single, easy to handle molecules. Short PEG chains were selected as spacers between the two peptide molecules, and a Cu(i)-catalyzed cycloaddition (CuAAC) protocol was used to assemble the final bis-PEG-peptide conjugate, by the convenient functionalization of PEG arms with azide and alkyne groups. The resulting conjugates, with a certain helical character in TFE solutions (CD), showed nanomolar affinity in a fluorescence CaM binding in vitro assay, higher than just the sum of the precursor PEG-peptide affinities, thus validating our design. The approach to these first described examples of Kv7.2 CaMBD-mimetics could pave the way to chimeric conjugates merging helices A and B from different Kv7 subunits. This journal is-
dc.description.sponsorshipThis research was supported by Consolider-Ingenio CSD2008-00005 (SICI to AV, RGM, and OM), BFU2012-39092-C02-02 (to RGM) and BFU2012-39883 (to AV). M.A.B. thanks the CSIC for a JAEdoc contract from the program “Junta para la Ampliación de Estudios”, co-financed by the ESF. A.A. was supported by Fundación Biofísica Bizkaia and by a Universidad del País Vasco (UPV/EHU) postdoctoral fellowship. C.M. was co-funded by the Spanish Ministry of Economy and Competitiveness (PTA2012) and by Fundación Biofísica Bizkaia.-
dc.publisherRoyal Society of Chemistry-
dc.rightsopenAccess-
dc.subjectPEG-peptide conjugates-
dc.subjectClick chemistry-
dc.subjectCalmodulin binding-
dc.subjectIon Channels-
dc.titleClicked bis-PEG-peptide conjugates for studying calmodulin-Kv7.2 channel binding-
dc.typeartículo-
dc.identifier.doi10.1039/c4ob01338g-
dc.date.updated2014-11-25T12:12:41Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
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