Unknown

Dataset Information

0

Designed to dissolve: suppression of colloidal aggregation of Cu(I)-selective fluorescent probes in aqueous buffer and in-gel detection of a metallochaperone.


ABSTRACT: Due to the lipophilicity of the metal-ion receptor, previously reported Cu(I)-selective fluorescent probes form colloidal aggregates, as revealed by dynamic light scattering. To address this problem, we have developed a hydrophilic triarylpyrazoline-based fluorescent probe, CTAP-2, that dissolves directly in water and shows a rapid, reversible, and highly selective 65-fold fluorescence turn-on response to Cu(I) in aqueous solution. CTAP-2 proved to be sufficiently sensitive for direct in-gel detection of Cu(I) bound to the metallochaperone Atox1, demonstrating the potential for cation-selective fluorescent probes to serve as tools in metalloproteomics for identifying proteins with readily accessible metal-binding sites.

SUBMITTER: Morgan MT 

PROVIDER: S-EPMC3388948 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Designed to dissolve: suppression of colloidal aggregation of Cu(I)-selective fluorescent probes in aqueous buffer and in-gel detection of a metallochaperone.

Morgan M Thomas MT   Bagchi Pritha P   Fahrni Christoph J CJ  

Journal of the American Chemical Society 20110914 40


Due to the lipophilicity of the metal-ion receptor, previously reported Cu(I)-selective fluorescent probes form colloidal aggregates, as revealed by dynamic light scattering. To address this problem, we have developed a hydrophilic triarylpyrazoline-based fluorescent probe, CTAP-2, that dissolves directly in water and shows a rapid, reversible, and highly selective 65-fold fluorescence turn-on response to Cu(I) in aqueous solution. CTAP-2 proved to be sufficiently sensitive for direct in-gel det  ...[more]

Similar Datasets

| S-EPMC8624267 | biostudies-literature
| S-EPMC6748674 | biostudies-literature
| S-EPMC7505426 | biostudies-literature
| S-EPMC8041305 | biostudies-literature
| S-EPMC5302499 | biostudies-literature
| S-EPMC5112770 | biostudies-literature
| S-EPMC9034144 | biostudies-literature
| S-EPMC3073858 | biostudies-literature
2012-03-31 | GSE28397 | GEO
| S-EPMC6538650 | biostudies-literature