Europium‐Labeled Activity‐Based Probe through Click Chemistry: Absolute Serine Protease Quantification Using <sup>153</sup>Eu Isotope Dilution ICP/MS

Yan, Xiaowen; Luo, Yacui; Zhang, Zhubao; Li, Laurent; Luo, Qiang; Yang, Limin; Zhang, Bo; Chen, Haifeng; Bai, Péter; Wang, Qiuquan

doi:10.1002/ange.201108277

Cited by 9 publications

(6 citation statements)

References 73 publications

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“…Among the handful of reported examples include a sulfonyl fluoride inhibitor of a-thrombin conjugated to a nitroxide spin label, [86] biotinylated [87] and alkyne-bearing [77] FSBA analogs for kinase profiling, a biotinylated sulfonyl fluoride probe for triglycerol lipases, [88] and a 153 Eu isotope-labeled probe for serine protease quantification. [89] Several recent examples of focused libraries of sulfonyl fluoride analogues of biologically active compounds have appeared, including aryl sulfonyl fluorides [90] and amino acid based sulfonyl fluorides [91] as serine protease inhibitors, a small set of amine aryl sulfonyl compounds as NADPH oxidase inhibitors, [92] long-chain alkyl sulfonyl fluorides as an outer membrane phospholipase A inhibitors, [93] and unsymmetrical urea derivatives as antimicrobial and antifungal agents. [94] All of the above factors, bolstered by our recent work in this area, [78] convince us that many more exciting applications lie ahead for the felicitous match of proteins with aryl sulfonyl fluorides.…”

Section: Methodsmentioning

confidence: 99%

Sulfur(VI) Fluoride Exchange (SuFEx): Another Good Reaction for Click Chemistry

et al. 2014

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Aryl sulfonyl chlorides (e.g. Ts-Cl) are beloved of organic chemists as the most commonly used S(VI) electrophiles, and the parent sulfuryl chloride, O2 S(VI) Cl2 , has also been relied on to create sulfates and sulfamides. However, the desired halide substitution event is often defeated by destruction of the sulfur electrophile because the S(VI) Cl bond is exceedingly sensitive to reductive collapse yielding S(IV) species and Cl(-) . Fortunately, the use of sulfur(VI) fluorides (e.g., R-SO2 -F and SO2 F2 ) leaves only the substitution pathway open. As with most of click chemistry, many essential features of sulfur(VI) fluoride reactivity were discovered long ago in Germany.6a Surprisingly, this extraordinary work faded from view rather abruptly in the mid-20th century. Here we seek to revive it, along with John Hyatt's unnoticed 1979 full paper exposition on CH2 CH-SO2 -F, the most perfect Michael acceptor ever found.98 To this history we add several new observations, including that the otherwise very stable gas SO2 F2 has excellent reactivity under the right circumstances. We also show that proton or silicon centers can activate the exchange of SF bonds for SO bonds to make functional products, and that the sulfate connector is surprisingly stable toward hydrolysis. Applications of this controllable ligation chemistry to small molecules, polymers, and biomolecules are discussed.

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Section: Methodsmentioning

confidence: 99%

Sulfur(VI) Fluoride Exchange (SuFEx): Another Good Reaction for Click Chemistry

et al. 2014

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“…One problem in addition to possible poor separation is unpredictable recovery . It has been shown that good separation of labeled proteins and antibodies is possible using RP and SEC columns with ICP‐MS detection, but not always in a straightforward manner …”

Section: Characterizationmentioning

confidence: 99%

Molecules and elements for quantitative bioanalysis: The allure of using electrospray, MALDI, and ICP mass spectrometry side‐by‐side

Linscheid

2018

Mass Spectrometry Reviews

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To understand biological processes, not only reliable identification, but quantification of constituents in biological processes play a pivotal role. This is especially true for the proteome: protein quantification must follow protein identification, since sometimes minute changes in abundance tell the real tale. To obtain quantitative data, many sophisticated strategies using electrospray and MALDI mass spectrometry (MS) have been developed in recent years. All of them have advantages and limitations. Several years ago, we started to work on strategies, which are principally capable to overcome some of these limits. The fundamental idea is to use elemental signals as a measure for quantities. We began by replacing the radioactive P with the "cold" natural P to quantify modified nucleotides and phosphorylated peptides and proteins and later used tagging strategies for quantification of proteins more generally. To do this, we introduced Inductively Coupled Plasma Mass Spectrometry (ICP-MS) into the bioanalytical workflows, allowing not only reliable and sensitive detection but also quantification based on isotope dilution absolute measurements using poly-isotopic elements. The detection capability of ICP-MS becomes particularly attractive with heavy metals. The covalently bound proteins tags developed in our group are based on the well-known DOTA chelate complex (1,4,7,10-tetraazacyclododecane-N,N',N″,N‴-tetraacetic acid) carrying ions of lanthanoides as metal core. In this review, I will outline the development of this mutual assistance between molecular and elemental mass spectrometry and discuss the scope and limitations particularly of peptide and protein quantification. The lanthanoide tags provide low detection limits, but offer multiplexing capabilities due to the number of very similar lanthanoides and their isotopes. With isotope dilution comes previously unknown accuracy. Separation techniques such as electrophoresis and HPLC were used and just slightly adapted workflows, already in use for quantification in bioanalysis. Imaging mass spectrometry (MSI) with MALDI and laser ablation ICP-MS complemented the range of application in recent years.

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“…Meanwhile, complete separation of analytes by chromatography/electrophoresis is a requisite prior to detection. To reduce the complexity of biological samples, activity-based probe was utilized by Wang et al 57 to provide biospecificity before chromatographic separation. It is demonstrated to be successful for serine proteases absolute quantification in real samples (human serum and rat tissue).…”

Section: Absolute Quantification Of Biomoleculesmentioning

confidence: 99%

Metal Stable Isotope Tagging: Renaissance of Radioimmunoassay for Multiplex and Absolute Quantification of Biomolecules

et al. 2016

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The unambiguous quantification of biomolecules is of great significance in fundamental biological research as well as practical clinical diagnosis. Due to the lack of a detectable moiety, the direct and highly sensitive quantification of biomolecules is often a "mission impossible". Consequently, tagging strategies to introduce detectable moieties for labeling target biomolecules were invented, which had a long and significant impact on studies of biomolecules in the past decades. For instance, immunoassays have been developed with radioisotope tagging by Yalow and Berson in the late 1950s. The later languishment of this technology can be almost exclusively ascribed to the use of radioactive isotopes, which led to the development of nonradioactive tagging strategy-based assays such as enzyme-linked immunosorbent assay, fluorescent immunoassay, and chemiluminescent and electrochemiluminescent immunoassay. Despite great success, these strategies suffered from drawbacks such as limited spectral window capacity for multiplex detection and inability to provide absolute quantification of biomolecules. After recalling the sequences of tagging strategies, an apparent question is why not use stable isotopes from the start? A reasonable explanation is the lack of reliable means for accurate and precise quantification of stable isotopes at that time. The situation has changed greatly at present, since several atomic mass spectrometric measures for metal stable isotopes have been developed. Among the newly developed techniques, inductively coupled plasma mass spectrometry is an ideal technique to determine metal stable isotope-tagged biomolecules, for its high sensitivity, wide dynamic linear range, and more importantly multiplex and absolute quantification ability. Since the first published report by our group, metal stable isotope tagging has become a revolutionary technique and gained great success in biomolecule quantification. An exciting research highlight in this area is the development and application of the mass cytometer, which fully exploited the multiplexing potential of metal stable isotope tagging. It realized the simultaneous detection of dozens of parameters in single cells, accurate immunophenotyping in cell populations, through modeling of intracellular signaling network and undoubted discrimination of function and connection of cell subsets. Metal stable isotope tagging has great potential applications in hematopoiesis, immunology, stem cells, cancer, and drug screening related research and opened a post-fluorescence era of cytometry. Herein, we review the development of biomolecule quantification using metal stable isotope tagging. Particularly, the power of multiplex and absolute quantification is demonstrated. We address the advantages, applicable situations, and limitations of metal stable isotope tagging strategies and propose suggestions for future developments. The transfer of enzymatic or fluorescent tagging to metal stable isotope tagging may occur in many aspects of biological and clinical practi...

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Europium‐Labeled Activity‐Based Probe through Click Chemistry: Absolute Serine Protease Quantification Using ¹⁵³Eu Isotope Dilution ICP/MS

Cited by 9 publications

References 73 publications

Sulfur(VI) Fluoride Exchange (SuFEx): Another Good Reaction for Click Chemistry

Sulfur(VI) Fluoride Exchange (SuFEx): Another Good Reaction for Click Chemistry

Molecules and elements for quantitative bioanalysis: The allure of using electrospray, MALDI, and ICP mass spectrometry side‐by‐side

Metal Stable Isotope Tagging: Renaissance of Radioimmunoassay for Multiplex and Absolute Quantification of Biomolecules

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Europium‐Labeled Activity‐Based Probe through Click Chemistry: Absolute Serine Protease Quantification Using 153Eu Isotope Dilution ICP/MS

Cited by 9 publications

References 73 publications

Sulfur(VI) Fluoride Exchange (SuFEx): Another Good Reaction for Click Chemistry

Sulfur(VI) Fluoride Exchange (SuFEx): Another Good Reaction for Click Chemistry

Molecules and elements for quantitative bioanalysis: The allure of using electrospray, MALDI, and ICP mass spectrometry side‐by‐side

Metal Stable Isotope Tagging: Renaissance of Radioimmunoassay for Multiplex and Absolute Quantification of Biomolecules

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Europium‐Labeled Activity‐Based Probe through Click Chemistry: Absolute Serine Protease Quantification Using ¹⁵³Eu Isotope Dilution ICP/MS