Development of a red fluorescent light-up probe for highly selective and sensitive detection of vicinal dithiol-containing proteins in living cells

Wang, Yuanyuan; Yang, Xiaofeng; Zhong, Yaogang; Gong, Xueyun; Li, Zheng; Li, Hua

doi:10.1039/c5sc02824h

Cited by 33 publications

(25 citation statements)

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“…In our continuing efforts to develop fluorescent probes for VDPs, we have developed a fluorogenic probe for specific detection of VDPs in living cells . However, the intensity-based probe is inferior to the ratiometric one, as the former is vulnerable to variations in the assay environment, thus posing potential problems for their use in quantitative measurements of VDPs in biological systems.…”

Section: Resultsmentioning

confidence: 99%

“…Because the removal of the unbound probes is unnecessary, real-time measurements and monitoring of molecular events in living cells is possible. In our earlier investigation, we created a light-up fluorescent probe for VDPs by adopting a fluorogenic mechanism based on an environment-sensitive fluorophore . Despite advances in the light-up fluorescent probes, they tend to be influenced by a variety of factors such as fluctuations in excitation intensity, environmental conditions, and the probe concentration.…”

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confidence: 99%

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Ratiometric Fluorescent Probe for Vicinal Dithiol-Containing Proteins in Living Cells Designed via Modulating the Intramolecular Charge Transfer–Twisted Intramolecular Charge Transfer Conversion Process

et al. 2016

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Vicinal dithiol-containing proteins (VDPs) play a significant role in maintaining the cellular redox homeostasis and are implicated in many diseases. To provide new chemical tools for VDPs imaging, we report here a ratiometric fluorescent probe CAsH2 for VDPs using 7-diethylaminiocoumarin as the fluorescent reporter and cyclic 1,3,2-dithiarsenolane as the specific ligand. CAsH2 shows peculiar dual fluorescence emission from the excited intramolecular charge transfer (ICT) and twisted intramolecular charge transfer (TICT) states in aqueous media. However, upon selective binding of protein vicinal dithiols to the trivalent arsenical of CAsH2, the probe was brought from the polar water media into the hydrophobic protein domain, causing the excited state ICT to TICT conversion to be restricted; as a result, an increase from the ICT emission band and a decrease from the TICT emission band were observed simultaneously. The designed probe shows high selectivity toward VDPs over other proteins and biological thiols. Preliminary experiments show that CAsH2 can be used for the ratiometric imaging of endogenous VDPs in living cells. So far as we know, this is a rare example of the ratiometric fluorescent probe designed via modulating the ICT-TICT conversion process, which provides a new way to construct various protein-specific ratiometric fluorescent probes.

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Section: Resultsmentioning

confidence: 99%

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Ratiometric Fluorescent Probe for Vicinal Dithiol-Containing Proteins in Living Cells Designed via Modulating the Intramolecular Charge Transfer–Twisted Intramolecular Charge Transfer Conversion Process

et al. 2016

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“… 143 , 144 Exofacial neighboring thiols have been imaged with such fluorescent arsonodithioite exchangers. 23 − 25 Phenyl arsine oxides were also shown early on to inhibit the entry of HIV virus about as efficiently as DTNB. 8 In clear contrast, thiol-mediated uptake and its inhibition remain a fascinating topic to be explored with dynamic covalent pnictogen chemistry, including possible contributions of turned-on noncovalent pnictogen bonds into deepened σ holes.…”

Section: Perspectivesmentioning

confidence: 99%

Thiol-Mediated Uptake

Laurent

Martinent

Lim

et al. 2021

JACS Au

110

208

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This Perspective focuses on thiol-mediated uptake, that is, the entry of substrates into cells enabled by oligochalcogenides or mimics, often disulfides, and inhibited by thiol-reactive agents. A short chronology from the initial observations in 1990 until today is followed by a summary of cell-penetrating poly(disulfide)s (CPDs) and cyclic oligochalcogenides (COCs) as privileged scaffolds in thiol-mediated uptake and inhibitors of thiol-mediated uptake as potential antivirals. In the spirit of a Perspective, the main part brings together topics that possibly could help to explain how thiol-mediated uptake really works. Extreme sulfur chemistry mostly related to COCs and their mimics, cyclic disulfides, thiosulfinates/-onates, diselenolanes, benzopolysulfanes, but also arsenics and Michael acceptors, is viewed in the context of acidity, ring tension, exchange cascades, adaptive networks, exchange affinity columns, molecular walkers, ring-opening polymerizations, and templated polymerizations. Micellar pores (or lipid ion channels) are considered, from cell-penetrating peptides and natural antibiotics to voltage sensors, and a concise gallery of membrane proteins, as possible targets of thiol-mediated uptake, is provided, including CLIC1, a thiol-reactive chloride channel; TMEM16F, a Ca-activated scramblase; EGFR, the epithelial growth factor receptor; and protein-disulfide isomerase, known from HIV entry or the transferrin receptor, a top hit in proteomics and recently identified in the cellular entry of SARS-CoV-2.

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“…In addition, applications of these probes in vivo have not been validated. Recently, some environmentally sensitive probes have been designed and synthesized for detecting VDPs. − These probes did not require tedious washing steps during protein imaging and exhibited fast fluorescence response, but they required a defined biology microenvironment of proteins, which limited their general applications.…”

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Decrease of Protein Vicinal Dithiols in Parkinsonism Disclosed by a Monoarsenical Fluorescent Probe

Jia

Hou

et al. 2020

Anal. Chem.

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Vicinal dithiol-containing proteins (VDPs) play an important role in maintaining the structures and functions of proteins mainly through the conversion between dithiols and disulfide bonds. The content of VDPs also reflects the redox status of an organism. To specifically and expediently detect VDPs, we developed a turn-on monoarsenical fluorescent probe (NEP) based on the intramolecular charge transfer mechanism. Naphthalimide was chosen as a fluorophore and linked with the receptor moiety (cyclic dithiarsolane) via carbamate segment. In the presence of VDPs, NEP displays a strong green fluorescence signal produced by the cyclic dithiarsolane cleavage and subsequent intramolecular cyclization to liberate the fluorophore. Furthermore, NEP exhibits high selectivity toward VDPs over other protein thiols and low molecular weight thiols. The favorable properties of NEP enable it readily to detect VDPs in live cells and in vivo. In addition, a remarkable decrease of VDPs in parkinsonism was disclosed for the first time, highlighting that regulating VDPs level has a therapeutic potential for parkinsonism.

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Development of a red fluorescent light-up probe for highly selective and sensitive detection of vicinal dithiol-containing proteins in living cells

Abstract: An environment-sensitive red fluorescent light-up probe for vicinal dithiol-containing proteins (VDPs) in living cells has been successfully developed.

Cited by 33 publications

References 50 publications

Ratiometric Fluorescent Probe for Vicinal Dithiol-Containing Proteins in Living Cells Designed via Modulating the Intramolecular Charge Transfer–Twisted Intramolecular Charge Transfer Conversion Process

Ratiometric Fluorescent Probe for Vicinal Dithiol-Containing Proteins in Living Cells Designed via Modulating the Intramolecular Charge Transfer–Twisted Intramolecular Charge Transfer Conversion Process

Thiol-Mediated Uptake

Decrease of Protein Vicinal Dithiols in Parkinsonism Disclosed by a Monoarsenical Fluorescent Probe

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