Storable Arylpalladium(II) Reagents for Alkene Labeling in Aqueous Media

Simmons, Rebecca; Yu, Robert T.; Myers, Andrew G.

doi:10.1021/ja206339s

Cited by 43 publications

(46 citation statements)

References 31 publications

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“…In conclusion, we have developed Pd-mediated siteselective S-arylation that exploits endogenous metal-binding motifs. In contrast to previous Pd-mediated bionconjugation reactions, 34,42,43 the isolation of a preformed Pd-aryl complex was not necessary and renders this protocol easy to implement. It also enables regioselective differentiation to enhance product homogeneity in proteins bearing multiple Cys.…”

Section: Scheme 1 Established Strategies Compared To Metalsite Guidementioning

confidence: 99%

Selective Metal-Site-Guided Arylation of Proteins

et al. 2016

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We describe palladium-mediated S-arylation that exploits natural metal-binding motifs to ensure high site selectivity for a proximal reactive residue. This allows the chemical identification not only of proteins that bind metals but also the environment of the metal-binding site itself through proteomic analysis of arylation sites. The transformation is easy to perform under standard conditions, does not require the isolation of a reactive Ar-Pd complex, is broad in scope, and is applicable in cell lysates as well as to covalent inhibition/modulation of metal-dependent enzymatic activity.

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Section: Scheme 1 Established Strategies Compared To Metalsite Guidementioning

confidence: 99%

Selective Metal-Site-Guided Arylation of Proteins

et al. 2016

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“…This compound was obtained in 82% yield; mp 217-221 °C; (reported: mp 165-166 °C) (Simmons et al, 2011). …”

Section: Expermental Methodsmentioning

confidence: 96%

Synthesis and evaluation of carbocyanine dyes as PRMT inhibitors and imaging agents

Sinha

Owens

Feng

et al. 2012

European Journal of Medicinal Chemistry

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Summary Protein arginine methylation regulates multiple biological processes. Deregulation of protein arginine methyltransferase (PRMT) activities has been observed in many disease phenotypes. Small molecule probes that target PRMTs with strong affinity and selectivity can be used as valuable tools to dissect biological mechanisms of arginine methylation and establish the role of PRMT proteins in a disease process. In this work, we report synthesis and evaluation of a class of carbocyanine compounds containing indolium, benz[e]indolium or benz[c,d]indolium heterocyclic moieties that bind to the predominant arginine methyltransferase PRMT1 and inhibit its methyltransferase activity at low micromolar potencies. In particular, the developed molecules have long wavelength colorimetric and fluorometric photoactivities, which can be used for optical and near-infrared fluorescence imaging in cells or biological tissues. Together, these new chemical probes have potential application in PRMT studies both as enzyme inhibitors and as fluorescent dyes for microscope imaging.

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“…Angeregt durch frühere Arbeiten zur Arylierung von Seleniden in kleinen Molekülen [214,215] entwickelten sie eine Methode zur Arylierung von oxidiertem Sec, wobei Boronsäurereagentien in einem Kupfer-vermittelten Prozess umgesetzt wurden. Zunächst wird einer der beiden Kupplungspartner an der gewünschte Positionen im Protein angebracht, und zwar in Form einer nichtnatürlichen Aminosäure durch chemische [216][217][218][219] oder enzymatische [220] Markierung,F estphasensynthese (solid-phase peptide synthesis,S PPS) [221,222] oder aber durch Erweiterung des genetischen Codes [223][224][225][226][227][228] (Ab-bildung 42). Aufd iese Weise konnte das in einem komplexen Peptid enthaltene Sec mit einer großen Vielfalt von Boronsäuren aryliert werden.…”

Section: Arylierung Oxidierter Selenocystein-elektrophileunclassified

Arylierungschemie für die Biokonjugation

et al. 2019

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Mittels Biokonjugationschemie können modifizierte Biomoleküle hergestellt werden, deren Funktionsumfang das natürliche Maß übersteigt. Hierbei ist die Entwicklung hocheffizienter und selektiver Biokonjugationsreaktionen von Bedeutung, die unter milden, biokompatiblen Bedingungen ablaufen. Vielversprechend sind hierbei Verfahren, bei denen Bindungen zwischen einem Nukleophil und einem sp2‐hybridisierten Kohlenstoffatom gebildet werden, wodurch in manchen Fällen Moleküle mit einzigartigen Eigenschaften erhalten werden können. In diesem Aufsatz werden Biokonjugationsstrategien für die Arylierung von Schwefel, Stickstoff, Selen, Sauerstoff und Kohlenstoff sowie ihre Anwendungen für die Modifikation von Peptiden, Proteinen, Kohlenhydraten und Nukleinsäuren zusammengefasst.

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Storable Arylpalladium(II) Reagents for Alkene Labeling in Aqueous Media

Cited by 43 publications

References 31 publications

Selective Metal-Site-Guided Arylation of Proteins

Selective Metal-Site-Guided Arylation of Proteins

Synthesis and evaluation of carbocyanine dyes as PRMT inhibitors and imaging agents

Arylierungschemie für die Biokonjugation

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