Catalytic Azide Reduction in Biological Environments

Sasmal, Pijus K.; Carregal‐Romero, Susana; Han, Alice A.; Streu, Craig; Lin, Zhijie; Namikawa, Kazuhiko; Elliott, Samantha; Köster, Reinhard W.; Parak, Wolfgang J.; Meggers, Eric

doi:10.1002/cbic.201100719

Cited by 116 publications

(104 citation statements)

References 40 publications

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“…Specifically, we synthesized SF4 by using a Sandmeyer reaction to convert commercially available rhodamine 110 into the bis-azido masked dye ( Fig. 1) (48). SF5 and SF7 were derived from carboxyrhodamine 1, which was prepared through the acid-mediated condensation of m-aminophenol with trimellitic anhydride.…”

Section: Resultsmentioning

confidence: 99%

Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H ₂ O ₂ -dependent H ₂ S production

Lin¹,

Lippert

Chang

2013

Proc. Natl. Acad. Sci. U.S.A.

343

223

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Hydrogen sulfide (H 2 S) is a reactive small molecule generated in the body that can be beneficial or toxic owing to its potent redox activity. In living systems, disentangling the pathways responsible for H 2 S production and their physiological and pathological consequences remains a challenge in part due to a lack of methods for monitoring changes in endogenous H 2 S fluxes. The development of fluorescent probes with appropriate selectivity and sensitivity for monitoring production of H 2 S at biologically relevant signaling levels offers opportunities to explore its roles in a variety of systems. Here we report the design, synthesis, and application of a family of azide-based fluorescent H 2 S indicators, Sulfidefluor-4, Sulfidefluor-5 acetoxymethyl ester, and Sulfidefluor-7 acetoxymethyl ester, which offer the unique capability to image H 2 S generated at physiological signaling levels. These probes are optimized for cellular imaging and feature enhanced sensitivity and cellular retention compared with our previously reported molecules. In particular, Sulfidefluor-7 acetoxymethyl ester allows for direct, real-time visualization of endogenous H 2 S produced in live human umbilical vein endothelial cells upon stimulation with vascular endothelial growth factor (VEGF). Moreover, we show that H 2 S production is dependent on NADPH oxidase-derived hydrogen peroxide (H 2 O 2 ), which attenuates VEGF receptor 2 phosphorylation and establishes a link for H 2 S/H 2 O 2 crosstalk. molecular imaging | redox biology | thiol | VEGFR

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Section: Resultsmentioning

confidence: 99%

Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H ₂ O ₂ -dependent H ₂ S production

Lin¹,

Lippert

Chang

2013

Proc. Natl. Acad. Sci. U.S.A.

343

223

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“…However, those reactions pass through a (thio)ester intermediate, so hydrolysis may compete with ligation (39,40). Artificial amino acids for bioorthogonal reaction would enable minimal modification but with some issues: the increased complexity of module expression and competing reactions [such as azide reduction (44), alkyne reaction with thiols (45), and spontaneous tetrazine degradation (46)] as well as competition from suppression of stop codons by normal amino acids (47). Recent work demonstrated the synthesis of ubiquitin homo-polymers by azide-alkyne (48), thiol-ene (49), or native chemical ligation reactions (50).…”

Section: Discussionmentioning

confidence: 99%

Programmable polyproteams built using twin peptide superglues

Veggiani

Nakamura

Brenner

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

269

360

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Programmed connection of amino acids or nucleotides into chains introduced a revolution in control of biological function. Reacting proteins together is more complex because of the number of reactive groups and delicate stability. Here we achieved sequenceprogrammed irreversible connection of protein units, forming polyprotein teams by sequential amidation and transamidation. SpyTag peptide is engineered to spontaneously form an isopeptide bond with SpyCatcher protein. By engineering the adhesin RrgA from Streptococcus pneumoniae, we developed the peptide SnoopTag, which formed a spontaneous isopeptide bond to its protein partner SnoopCatcher with >99% yield and no crossreaction to SpyTag/SpyCatcher. Solid-phase attachment followed by sequential SpyTag or SnoopTag reaction between building-blocks enabled iterative extension. Linear, branched, and combinatorial polyproteins were synthesized, identifying optimal combinations of ligands against death receptors and growth factor receptors for cancer cell death signal activation. This simple and modular route to programmable "polyproteams" should enable exploration of a new area of biological space.synthetic biology | protein engineering | nanobiotechnology | split protein | antibody

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“…HPLC‐MS : Genetically encoded azides are susceptible to in vivo reduction . Therefore, DTT (20 m m ) was added after labeling to obtain homogeneous samples for mass evaluation.…”

Section: Methodsmentioning

confidence: 99%

A FRET Sensor to Monitor Bivalent SUMO–SIM Interactions in SUMO Chain Binding

Kost

Mootz

2017

ChemBioChem

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The small ubiquitin-like modifier (SUMO) can be assembled into polymeric chains as part of its diverse biochemical signal pattern upon conjugation to substrate proteins. SUMO chain recognition is facilitated by receptor proteins that contain at least two SUMO-interacting motifs (SIMs). Little is known about the structure of SUMO chains, both in an unliganded form and upon complexation with multi-SIM protein partners. A FRET sensor has been developed based on a linear dimer of human SUMO-2 as a minimal SUMO chain analogue. The synthetic acceptor and donor dyes were conjugated by maleimide and copper-catalyzed click chemistry to each of the two SUMO subunits. FRET changes were only observed in the presence of di- or multi-SIM ligands. Alteration of the short linker sequence between SIMs 2 and 3 of RNF4 showed a great tolerance, and hence, structural flexibility, of the SUMO dimer for bivalent binding of adjacent SIMs. The di-SUMO FRET sensor reports on the binding of SIM clusters of the proteins C5orf25 and SOBP; this suggest that these can bind to adjacent subunits of a SUMO chain. The developed FRET sensor will be a useful tool to study the importance of SIM and linker sequences, as well as biochemical and structural properties of SUMO chains and multi-SIM proteins.

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Catalytic Azide Reduction in Biological Environments

Cited by 116 publications

References 40 publications

Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H ₂ O ₂ -dependent H ₂ S production

Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H ₂ O ₂ -dependent H ₂ S production

Programmable polyproteams built using twin peptide superglues

A FRET Sensor to Monitor Bivalent SUMO–SIM Interactions in SUMO Chain Binding

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Catalytic Azide Reduction in Biological Environments

Cited by 116 publications

References 40 publications

Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H 2 O 2 -dependent H 2 S production

Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H 2 O 2 -dependent H 2 S production

Programmable polyproteams built using twin peptide superglues

A FRET Sensor to Monitor Bivalent SUMO–SIM Interactions in SUMO Chain Binding

Contact Info

Product

Resources

About

Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H ₂ O ₂ -dependent H ₂ S production

Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H ₂ O ₂ -dependent H ₂ S production