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Clicked bis-PEG-peptide Conjugates for Studying calmodulin-Kv7.2 Channel Binding

Clicked bis-PEG-peptide Conjugates for Studying calmodulin-Kv7.2 Channel Binding

M Angeles Bonache, Alessandro Alaimo, Covadonga Malo, Oscar Millet, Alvaro Villarroel, Rosario González-Muñiz

Org Biomol Chem. 2014 Nov 28;12(44):8877-87.

PMID: 25264745

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP82055945-A	Polyoxyethylene bis(azide)		82055-94-5	Price

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