Colloidal Fluorophore Aggregates for the Selective Detection of Albumins in Solution and on Electrophoresis Gels

Park, Ji-Hee; Kim, Youngmi

doi:10.1002/cbic.201800608

Cited by 12 publications

(6 citation statements)

References 61 publications

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“…For example, the fluorescence intensity at 538 nm increases 18‐fold ( F / F 0 ) in viscous glycerol relative to that of fluid ethanol solution (Figure 6b). Moreover, a related target binding‐induced deaggregation and rigidification has previously been invoked to rationalize the fluorogenic responses of CV derivatives in the presence of other biomacromolecules [65] …”

Section: Resultsmentioning

confidence: 99%

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Self‐Assembled Peptidyl Aggregates for the Fluorogenic Recognition of Mitochondrial DNA G‐Quadruplexes

et al. 2022

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The selective monitoring of G-quadruplex (G4) structures in living cells is important to elucidate their functions and reveal their value as diagnostic or therapeutic targets. Here we report a fluorogenic probe (CV2) able to selectively light-up parallel G4 DNA over antiparallel topologies. CV2 was constructed by conjugating the excimer-forming CV dye with a peptide sequence (L-Arg-L-Gly-glutaric acid) that specifically recognizes G4s. CV2 forms self-assembled, red excimeremitting nanoaggregates in aqueous media, but specific binding to G4s triggers its disassembly into rigidified monomeric dyes, leading to a dramatic fluorescence enhancement. Moreover, selective permeation of CV2 stains G4s in mitochondria over the nucleus. CV2 was employed for tracking the folding and unfolding of G4s in living cells, and for monitoring mitochondrial DNA (mtDNA) damage. These properties make CV2 appealing to investigate the possible roles of mtDNA G4s in diseases that involve mitochondrial dysfunction.

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Section: Resultsmentioning

confidence: 99%

“…Moreover, a related target binding-induced deaggregation and rigidification has previously been invoked to rationalize the fluorogenic responses of CV derivatives in the presence of other biomacromolecules. [65]…”

Section: Photophysical Underpinnings Of the Fluorogenic Responsementioning

confidence: 99%

Self‐Assembled Peptidyl Aggregates for the Fluorogenic Recognition of Mitochondrial DNA G‐Quadruplexes

et al. 2022

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“…Related cyanine dyes were recently described by Park et al [35] that are said to respond to serum albumins via the disassembly of fluorescence-quenched aggregates of dyes 1, 2 and 3 as shown in figure 4. It cannot be excluded, though, that the effects additionally are caused by the replacement of the cyano groups (which have a reactivity close to that of some chloro substitutents) with lysine amino groups in the albumins.…”

Section: Polymethine Chameleon Labelsmentioning

confidence: 99%

Fluorescent chameleon labels for bioconjugation and imaging of proteins, nucleic acids, biogenic amines and surface amino groups. a review

Wolfbeis

2021

Methods Appl. Fluoresc.

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Chameleon labels (ChLs) possess the unique property of changing (visible) color and fluorescence on binding to amino groups of biomolecules. MostChLs react with primary aliphatic amino groups such as those in lysine or with amino groups artificially introduced into polynucleic acids or saccharides, but someothers also react with secondary amino groups. Under controlled circumstances, the reactions are fairly specific. The review is subdivided into the following sections: (1) An introduction and classification of fluorescent labels; (2) pyrylium labels that undergo shortwave color changes upon labelling, typically from blue to red; (3) polymethine type of labels (that also undergo shortwave color changes, typically from green to blue; (4) various other (less common) chromogenic and fluorogenic systems; (5) hemicyanine labels that undergo longwave color changes, typically from yellow to purple; (6) the application of ChLs to labeling of proteins and oligonucleotides; (7) applications to fluorometric assays and sensing; (8) applications to fluorescence imaging of biomolecules; (9) applications in studies on affinity interactions (receptor-ligand binding); (10) applications in surface and interface chemistry; and (11) applications in chromatography, electrophoresis and isotachophoresis of biomolecules.

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“…Because of the amphoteric behavior of histidine at neutral pH, it can easily participate in the π interactions with other amino acids and cations in proteins . Involving the imidazole ring in the catalytic sites of many metalloproteins and enzymes, histidine directly plays important roles in human biochemistry. − Misregulation in the levels of histidine-rich proteins is connected to several diseases, such as liver cirrhosis, low heart function, malaria, genetic thrombophilia, AIDS, renal diseases, pulmonary disorders, asthma, etc. − Different techniques such as immunoassays, − colorimetry, fluorescence, , high performance liquid chromatography (HPLC), and thin-layer or gas chromatography − are available for detecting histidine and histidine-rich proteins. Although reports ae available on detecting human serum albumin (HSA) or bovine serum albumin (BSA), a few articles reported fluorescence turn-on sensing of various histidine-rich proteins. ,, For example, Wong et al reported a luminescent iridium complex as a histidine-specific probe used to stain histidine-rich proteins .…”

Section: Introductionmentioning

confidence: 99%

A Water-Soluble Wavy Coordination Polymer of Cu(II) as a Turn-On Luminescent Probe for Histidine and Histidine-Rich Proteins/Peptides

Ghosh,

Nair,

Ghosh

et al. 2024

Inorg. Chem.

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Histidine plays an essential role in most biological systems. Changes in the homeostasis of histidine and histidine-rich proteins are connected to several diseases. Herein, we report a water-soluble Cu(II) coordination polymer, labeled CuCP, for the fluorimetric detection of histidine and histidine-rich proteins and peptides. Single-crystal structure determination of CuCP revealed a two-dimensional wavy network structure in which a carboxylate group connects the individual Cu(II) dimer unit in a syn−anti conformation. The weakly luminescent and water-soluble CuCP shows turn-on blue emission in the presence of histidine and histidine-rich peptides and proteins. The polymer can also stain histidine-rich proteins via gel electrophoresis. The limits of quantifications for histidine, glycine-histidine, serine-histidine, human serum albumin (HSA), bovine serum albumin, pepsin, trypsin, and lysozyme were found to be 300, 160, 600, 300, 600, 800, 120, and 290 nM, respectively. Utilizing the fluorescence turn-on property of CuCP, we measured HSA quantitatively in the urine samples. We also validated the present urinary HSA measurement assay with existing analytical techniques. Job's plot, 1 H NMR, high-resolution mass spectrometry (HRMS), electron paramagnetic resonance (EPR), fluorescence, and UV−vis studies confirmed the ligand displacement from CuCP in the presence of histidine.

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Colloidal Fluorophore Aggregates for the Selective Detection of Albumins in Solution and on Electrophoresis Gels

Cited by 12 publications

References 61 publications

Self‐Assembled Peptidyl Aggregates for the Fluorogenic Recognition of Mitochondrial DNA G‐Quadruplexes

Self‐Assembled Peptidyl Aggregates for the Fluorogenic Recognition of Mitochondrial DNA G‐Quadruplexes

Fluorescent chameleon labels for bioconjugation and imaging of proteins, nucleic acids, biogenic amines and surface amino groups. a review

A Water-Soluble Wavy Coordination Polymer of Cu(II) as a Turn-On Luminescent Probe for Histidine and Histidine-Rich Proteins/Peptides

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