N’-acyl-N-methylphenylenediamine as a novel proximity labeling agent for signal amplification in immunohistochemistry

Sato, Shinichi; Yoshida, Masaki; Hatano, Kensuke; Matsumura, Masaki; Nakamura, Hiroyuki

doi:10.1016/j.bmc.2019.01.036

Cited by 11 publications

(8 citation statements)

References 22 publications

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“…PDL has emerged as a powerful approach for mapping protein–protein interactions, spatial transcriptomes, and site-selective protein labeling. Highly reactive species such as radicals, − carbene, , metallocarbene, and activated electrophilic species have been reported.…”

Section: Introductionmentioning

confidence: 99%

Proximity Histidine Labeling by Umpolung Strategy Using Singlet Oxygen

et al. 2021

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While electrophilic reagents for histidine labeling have been developed, we report an umpolung strategy for histidine functionalization. A nucleophilic small molecule, 1-methyl-4-arylurazole, selectively labeled histidine under singlet oxygen (1O2) generation conditions. Rapid histidine labeling can be applied for instant protein labeling. Utilizing the short diffusion distance of 1O2 and a technique to localize the 1O2 generator, a photocatalyst in close proximity to the ligand-binding site, we demonstrated antibody Fc-selective labeling on magnetic beads functionalized with a ruthenium photocatalyst and Fc ligand, ApA. Three histidine residues located around the ApA binding site were identified as labeling sites by liquid chromatography–mass spectrometry analysis. This result suggests that 1O2-mediated histidine labeling can be applied to a proximity labeling reaction on the nanometer scale.

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Section: Introductionmentioning

confidence: 99%

Proximity Histidine Labeling by Umpolung Strategy Using Singlet Oxygen

et al. 2021

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“…In a recent study this chemistry was extended to immunohistochemistry applications. 108 After the basic chemistry was established using peptides, the shift to proteins was made. Sato and Nakamura also showed for these much more complex biomolecules that in situ activation of functionalized N-methyl luminol (NML) derivatives by means of hemin (redox potential: −0.35 V) and H 2 O 2 led to substantially cleaner modification of Tyr residues when compared to the application of PTAD.…”

Section: Tyrosinementioning

confidence: 99%

Oxidation-Induced “One-Pot” Click Chemistry

et al. 2021

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Click chemistry has been established rapidly as one of the most valuable methods for the chemical transformation of complex molecules. Due to the rapid rates, clean conversions to the products, and compatibility of the reagents and reaction conditions even in complex settings, it has found applications in many molecule-oriented disciplines. From the vast landscape of click reactions, approaches have emerged in the past decade centered around oxidative processes to generate in situ highly reactive synthons from dormant functionalities. These approaches have led to some of the fastest click reactions know to date. Here, we review the various methods that can be used for such oxidation-induced “one-pot” click chemistry for the transformation of small molecules, materials, and biomolecules. A comprehensive overview is provided of oxidation conditions that induce a click reaction, and oxidation conditions are orthogonal to other click reactions so that sequential “click-oxidation-click” derivatization of molecules can be performed in one pot. Our review of the relevant literature shows that this strategy is emerging as a powerful approach for the preparation of high-performance materials and the generation of complex biomolecules. As such, we expect that oxidation-induced “one-pot” click chemistry will widen in scope substantially in the forthcoming years.

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“…1C). For example, controlling the tyramide-utilizing modification reaction around horseradish peroxidase (HRP)-conjugated antibodies has been applied to the signal amplification technique for immunostaining [64][65][66][67] and to analyze the clustering of membrane proteins on the cell membrane. 68) In addition, the APEX method, 69,70) which utilizes an engineered peroxidase that is active even in the intracellular environment to label proteins 20 nm around the enzyme with tyramide, has been developed as a technique to comprehensively reveal the cellular localization of proteins at the sub-organelle level and has been actively applied in recent years.…”

Section: Reviewmentioning

confidence: 99%

Protein Chemical Modification Using Highly Reactive Species and Spatial Control of Catalytic Reactions

Sato

2022

CHEMICAL & PHARMACEUTICAL BULLETIN

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Protein bioconjugation has become an increasingly important research method for introducing artificial functions in to protein with various applications, including therapeutics and biomaterials. Due to its amphiphilic nature, only a few tyrosine residues are exposed on the protein surface. Therefore, tyrosine residue has attracted attention as suitable targets for site-specific modification, and it is the most studied amino acid residue for modification reactions other than lysine and cysteine residues. In this review, we present the progress of our tyrosine chemical modification studies over the past decade. We have developed several different catalytic approaches to selectively modify tyrosine residues using peroxidase, laccase, hemin, and ruthenium photocatalysts. In addition to modifying tyrosine residues by generating radical species through single-electron transfer, we have developed a histidine modification method that utilizes singlet oxygen generated by photosensitizers. These highly reactive chemical species selectively modify proteins in close proximity to the enzyme/catalyst. Taking advantage of the spatially controllable reaction fields, we have developed novel methods for site-specific antibody modification, detecting hotspots of oxidative stress, and target identification of bioactive molecules.

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N’-acyl-N-methylphenylenediamine as a novel proximity labeling agent for signal amplification in immunohistochemistry

Cited by 11 publications

References 22 publications

Proximity Histidine Labeling by Umpolung Strategy Using Singlet Oxygen

Proximity Histidine Labeling by Umpolung Strategy Using Singlet Oxygen

Oxidation-Induced “One-Pot” Click Chemistry

Protein Chemical Modification Using Highly Reactive Species and Spatial Control of Catalytic Reactions

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