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Título: | Clicked bis-PEG-peptide conjugates for studying calmodulin-Kv7.2 channel binding |
Autor: | Bonache de Marcos, María Ángeles CSIC ORCID ; Alaimo, Alessandro CSIC ORCID; Malo, Covadonga CSIC ORCID; Millet, Oscar; Villarroel, Álvaro CSIC ORCID; González-Muñiz, Rosario CSIC ORCID | Palabras clave: | PEG-peptide conjugates Click chemistry Calmodulin binding Ion Channels |
Fecha de publicación: | 2014 | Editor: | Royal Society of Chemistry (UK) | Citación: | Organic and Biomolecular Chemistry 12: 8877- 8887 (2014) | Resumen: | The 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 | URI: | http://hdl.handle.net/10261/108026 | DOI: | 10.1039/c4ob01338g | Identificadores: | doi: 10.1039/c4ob01338g issn: 1477-0520 e-issn: 1477-0539) |
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