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Clicked bis-PEG-peptide conjugates for studying calmodulin-Kv7.2 channel binding

AuthorsBonache de Marcos, María Ángeles CSIC ORCID ; Alaimo, Alessandro; Malo, Covadonga; Millet, Oscar; Villarroel, Alvaro; González-Muñiz, Rosario CSIC ORCID
KeywordsPEG-peptide conjugates
Click chemistry
Calmodulin binding
Ion Channels
Issue Date2014
PublisherRoyal Society of Chemistry (UK)
CitationOrganic and Biomolecular Chemistry 12: 8877- 8887 (2014)
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
Identifiersdoi: 10.1039/c4ob01338g
issn: 1477-0520
e-issn: 1477-0539)
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