Switchable Zinc (II)-Responsive Globular β-Sheet Peptide [Research Data]

DOI

The natural function of many proteins depends on their ability to switch their conformation driven by environmental changes. In this work, we present a small, monomeric β-sheet peptide that switches between a molten globule and a folded state through Zn(II) binding. The solvent-exposed hydrophobic core on the β-sheet surface was substituted by a His3-site, whereas the internal hydrophobic core was left intact. Zn(II) is specifically recognized by the peptide relative to other divalent metal ions, binds in the lower micromolar range, and can be removed and re-added without denaturation of the peptide. In addition, the peptide is fully pH-switchable, has a pKa of about 6, and survives several cycles of acidification and neutralization. In-depth structural characterization of the switch was achieved by concerted application of circular dichroism (CD) and multinuclear NMR spectroscopy. Thus, this study represents a viable approach toward a globular β-sheet Zn(II) mini-receptor prototype.

Identifier
DOI https://doi.org/10.11588/data/HV4MJW
Related Identifier https://doi.org/10.1021/acssynbio.1c00396
Metadata Access https://heidata.uni-heidelberg.de/oai?verb=GetRecord&metadataPrefix=oai_datacite&identifier=doi:10.11588/data/HV4MJW
Provenance
Creator Pham, Truc Lam (Heidelberg University, Institute of Organic Chemistry); Kovermann, Michael (University of Konstanz, Department of Chemistry); Thomas, Franziska (Heidelberg University, Institute of Organic Chemistry)
Publisher heiDATA
Contributor Thomas, Franziska
Publication Year 2022
Rights Data are licensed under <a href='http://creativecommons.org/licenses/by/4.0/'>Creative Commons Attribution 4.0 International License &#160;<img src='https://i.creativecommons.org/l/by/4.0/80x15.png' alt='CC by' /></a>.; info:eu-repo/semantics/openAccess
OpenAccess true
Contact Thomas, Franziska (Heidelberg University, Institute of Organic Chemistry)
Representation
Resource Type Dataset
Format application/zip; application/pdf
Size 1856242; 114604592; 364336; 2811785; 246254
Version 1.1
Discipline Chemistry;Engineering