DNA can be oxidatively cleaved by copper complexes of the ATCUN peptide (amino terminal Cu(II)- and Ni(II)-binding motif). In order to investigate the fate of the metal ion throughout this process, we have exploited quenching/dequenching effects of conjugated fluorophores.
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Fluorescence Labeling of Peptides: Finding the Optimal Protocol for Coupling Various Dyes to ATCUN-like Structures.
ACS Org Inorg Au
October 2024
Department of Chemistry and Molecular Biology, Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, Medicinaregatan 7B, Gothenburg 413 90, Sweden.
Labeling of peptides and proteins with fluorescent dyes is a key step in functionalizing these structures for a wide array of biological assays. However, coupling strategies of such dyes have not been optimized for the most common compounds, while this step is typically the most precious and costly of the whole synthesis. We searched for the best conditions for attachment of the most widely used fluorescent dyes such as 6-carboxyfluorescein, Rhodamine B, and BODIPY-FL to peptides, where amino terminal Cu(II) and Ni(II) binding site (ATCUN) peptides were used as a model system.
View Article and Find Full Text PDFDesigned Metal-ATCUN Derivatives: Redox- and Non-redox-Based Applications Relevant for Chemistry, Biology, and Medicine.
iScience
December 2020
LAQV-REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Campus de Caparica, 2829-516 Caparica, Portugal.
The designed "ATCUN" motif (amino-terminal copper and nickel binding site) is a replica of naturally occurring ATCUN site found in many proteins/peptides, and an attractive platform for multiple applications, which include nucleases, proteases, spectroscopic probes, imaging, and small molecule activation. ATCUN motifs are engineered at periphery by conjugation to recombinant proteins, peptides, fluorophores, or recognition domains through chemically or genetically, fulfilling the needs of various biological relevance and a wide range of practical usages. This chemistry has witnessed significant growth over the last few decades and several interesting ATCUN derivatives have been described.
View Article and Find Full Text PDFA high-affinity fluorescence probe for copper(II) ions and its application in fluorescence lifetime correlation spectroscopy.
Anal Bioanal Chem
June 2019
Department of Biophysical Chemistry, Saarland University, Campus B2 2, 66123, Saarbrücken, Germany.
Copper is one of the most important transition metals in many organisms where it catalyzes a manifold of different processes. As a result of copper's redox activity, organisms have to avoid unbound ions, and a dysfunctional copper homeostasis may lead to multifarious pathological processes in cells with very severe ramifications for the affected organisms. In many neurodegenerative diseases, however, the exact role of copper ions is still not completely clarified.
View Article and Find Full Text PDFFluorophore ATCUN complexes: combining agent and probe for oxidative DNA cleavage.
Chem Commun (Camb)
August 2015
Institut für Chemie und Biochemie, Freie Universität Berlin, Fabeckstr. 34/36, 14195 Berlin, Germany.
DNA can be oxidatively cleaved by copper complexes of the ATCUN peptide (amino terminal Cu(II)- and Ni(II)-binding motif). In order to investigate the fate of the metal ion throughout this process, we have exploited quenching/dequenching effects of conjugated fluorophores.
View Article and Find Full Text PDFThe switch-on luminescence sensing of histidine-rich proteins in solution: a further application of a Cu2+ ligand.
Org Biomol Chem
June 2011
State Key Laboratory of Supramolecular Structure and Materials, Jilin University, No. 2699, Qianjin Street, Changchun, 130012, China.
A new probe/Cu(2+) complex for the detection of his-tagged protein has been developed, based on an improved probe, Dansyl-Gly-Py (1), by closely mimicing the structure of a peptide, ATCUN. In aqueous solution, 1/Cu(2+) has good selectivity to histidine and cysteine, and further can detect histidine-rich protein by releasing the quenched fluorescence of 1.
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