Journal of the American Chemical Society · 2006 · 167 citations · 23 references
Life SciencesBiochemistryMolecular BiologyMolecular BiophysicsMolecular ImagingMolecular RecognitionLigand BindingMolecular Probe DevelopmentProtein-ligand BindingProtein-ligand InteractionsProtein-ligand RecognitionReceptor-ligand InteractionsAffinity-based ProbesIsothermal Titration CalorimetryMolecular Fluorescence ImagingMolecular Imaging Probe DesignPeptide-based ProbesProtein-based Imaging AgentsProtein-specific LabelingZinc(ii) Recognition
To accomplish the selective labeling of a specific protein in complicated biological systems, a peptide tag incorporated into the protein and a complementary small molecular probe are required. Although a variety of peptide tag/probe pairs have been developed as molecular tools for protein analyses, the availability of pairs suitable for real-time imaging of proteins is still limited. We now report a new peptide tag/artificial probe pair composed of a genetically encodable oligo-aspartate sequence (D4 tag, (D4)n, n = 1-3) and the corresponding multinuclear Zn(II) complexes (Zn(II)-DpaTyrs). The strong binding affinity of the Zn(II)-DpaTyr probes with the D4 tag was a result of the multiple coordination bonds and the multivalent effect. It was measured quantitatively by isothermal titration calorimetry. The high affinity between the tag and the probe, indispensable for the selective protein labeling, enabled the pair to be used for the labeling and fluorescence imaging of a membrane-bound receptor protein tethering a triply repeated D4 tag ((D4)3) in an intact cell configuration without significantly affecting the receptor signal transduction.
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Multicolor and Electron Microscopic Imaging of Connexin Trafficking
Guido Gaietta, Thomas J. Deerinck, Stephen Adams et al. · Science · 2002 · 901 citations