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We began analyzing https://www.nature.com/articles/srep43135, but it redirected us to https://www.nature.com/articles/srep43135. The analysis below is for the second page.

Title[redir]:
Highly sensitive and adaptable fluorescence-quenched pair discloses the substrate specificity profiles in diverse protease families | Scientific Reports
Description:
Internally quenched fluorescent (IQF) peptide substrates originating from FRET (Förster Resonance Energy Transfer) are powerful tool for examining the activity and specificity of proteases, and a variety of donor/acceptor pairs are extensively used to design individual substrates and combinatorial libraries. We developed a highly sensitive and adaptable donor/acceptor pair that can be used to investigate the substrate specificity of cysteine proteases, serine proteases and metalloproteinases. This novel pair comprises 7-amino-4-carbamoylmethylcoumarin (ACC) as the fluorophore and 2,4-dinitrophenyl-lysine (Lys(DNP)) as the quencher. Using caspase-3, caspase-7, caspase-8, neutrophil elastase, legumain, and two matrix metalloproteinases (MMP2 and MMP9), we demonstrated that substrates containing ACC/Lys(DNP) exhibit 7 to 10 times higher sensitivity than conventional 7-methoxy-coumarin-4-yl acetic acid (MCA)/Lys(DNP) substrates; thus, substantially lower amounts of substrate and enzyme can be used for each assay. We therefore propose that the ACC/Lys(DNP) pair can be considered a novel and sensitive scaffold for designing substrates for any group of endopeptidases. We further demonstrate that IQF substrates containing unnatural amino acids can be used to investigate protease activities/specificities for peptides containing post-translationally modified amino acids. Finally, we used IQF substrates to re-investigate the P1-Asp characteristic of caspases, thus demonstrating that some human caspases can also hydrolyze substrates after glutamic acid.

Matching Content Categories {📚}

  • Education
  • Science
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Content Management System {📝}

What CMS is doi.org built with?

Custom-built

No common CMS systems were detected on Doi.org, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of doi.org audience?

🏙️ Massive Traffic: 50M - 100M visitors per month


Based on our best estimate, this website will receive around 80,479,999 visitors per month in the current month.

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How Does Doi.org Make Money? {💸}

We can't see how the site brings in money.

The purpose of some websites isn't monetary gain; they're meant to inform, educate, or foster collaboration. Everyone has unique reasons for building websites. This could be an example. Doi.org could be secretly minting cash, but we can't detect the process.

Keywords {🔍}

caspase, substrates, article, substrate, pubmed, google, scholar, cas, doi, specificity, quenched, concentration, acc, internally, caspases, glu, enzyme, nature, pair, protease, iqf, mmp, fluorescence, trypsin, proteases, mca, cleavage, peptide, amino, cell, activity, residues, assay, enzymes, asp, library, libraries, acids, size, buffer, analysis, human, kinetic, central, full, gly, ranged, preferences, fluorophore, elastase,

Topics {✒️}

nature portfolio privacy policy 7-methoxy-coumarin-4-yl acetic acid-2 author information authors full-length substrate acc-gdevdgvk membrane-bound collagenase mt1-mmp advertising general formula acc-gglsxivk social media canada research chair chemical tools hydrophobic nature nature methods 12 nature methods 2 protease-based drug discovery 0/ reprints nature nature 410 izabela rutkowska-wlodarczyk atherosclerosis-based cardiovascular disease conserved xiap-interaction motif caspase substrate acc-gdevdgvk horizon 2020 research blood research designed research p1-asp/glu substrate libraries solid-phase library synthesis excellent tools full size image performed research synthesizing fluorophore-gdevdgvk 1 μm solutions develop substrate-based markers50 p1-p3 peptide libraries solid-phase peptide synthesis itraq-tails quantitative proteomics interleukin-1-beta converting-enzyme multiplex n-terminome analysis pair comprises 7-amino-4-carbamoylmethylcoumarin post-translationally modified residues adaptable donor/acceptor pair post-translationally modified lysine post-translationally modified peptides apoptotic cell-based experiments post-translationally modified arginine donor/acceptor pair acc/dnp acc/dnp donor/acceptor pair d-amino acid inhibitors full size table c-terminal glu residues45

Questions {❓}

  • Matrix metalloproteinases: what do they not do?

Schema {🗺️}

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         description:Internally quenched fluorescent (IQF) peptide substrates originating from FRET (Förster Resonance Energy Transfer) are powerful tool for examining the activity and specificity of proteases, and a variety of donor/acceptor pairs are extensively used to design individual substrates and combinatorial libraries. We developed a highly sensitive and adaptable donor/acceptor pair that can be used to investigate the substrate specificity of cysteine proteases, serine proteases and metalloproteinases. This novel pair comprises 7-amino-4-carbamoylmethylcoumarin (ACC) as the fluorophore and 2,4-dinitrophenyl-lysine (Lys(DNP)) as the quencher. Using caspase-3, caspase-7, caspase-8, neutrophil elastase, legumain, and two matrix metalloproteinases (MMP2 and MMP9), we demonstrated that substrates containing ACC/Lys(DNP) exhibit 7 to 10 times higher sensitivity than conventional 7-methoxy-coumarin-4-yl acetic acid (MCA)/Lys(DNP) substrates; thus, substantially lower amounts of substrate and enzyme can be used for each assay. We therefore propose that the ACC/Lys(DNP) pair can be considered a novel and sensitive scaffold for designing substrates for any group of endopeptidases. We further demonstrate that IQF substrates containing unnatural amino acids can be used to investigate protease activities/specificities for peptides containing post-translationally modified amino acids. Finally, we used IQF substrates to re-investigate the P1-Asp characteristic of caspases, thus demonstrating that some human caspases can also hydrolyze substrates after glutamic acid.
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      headline:Highly sensitive and adaptable fluorescence-quenched pair discloses the substrate specificity profiles in diverse protease families
      description:Internally quenched fluorescent (IQF) peptide substrates originating from FRET (Förster Resonance Energy Transfer) are powerful tool for examining the activity and specificity of proteases, and a variety of donor/acceptor pairs are extensively used to design individual substrates and combinatorial libraries. We developed a highly sensitive and adaptable donor/acceptor pair that can be used to investigate the substrate specificity of cysteine proteases, serine proteases and metalloproteinases. This novel pair comprises 7-amino-4-carbamoylmethylcoumarin (ACC) as the fluorophore and 2,4-dinitrophenyl-lysine (Lys(DNP)) as the quencher. Using caspase-3, caspase-7, caspase-8, neutrophil elastase, legumain, and two matrix metalloproteinases (MMP2 and MMP9), we demonstrated that substrates containing ACC/Lys(DNP) exhibit 7 to 10 times higher sensitivity than conventional 7-methoxy-coumarin-4-yl acetic acid (MCA)/Lys(DNP) substrates; thus, substantially lower amounts of substrate and enzyme can be used for each assay. We therefore propose that the ACC/Lys(DNP) pair can be considered a novel and sensitive scaffold for designing substrates for any group of endopeptidases. We further demonstrate that IQF substrates containing unnatural amino acids can be used to investigate protease activities/specificities for peptides containing post-translationally modified amino acids. Finally, we used IQF substrates to re-investigate the P1-Asp characteristic of caspases, thus demonstrating that some human caspases can also hydrolyze substrates after glutamic acid.
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      name:Department of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology, Wyb, Wyspianskiego 27, Poland
      name:Department of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology, Wyb, Wyspianskiego 27, Poland
      name:Department of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology, Wyb, Wyspianskiego 27, Poland
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      name:Kennedy Institute of Rheumatology, University of Oxford, United Kingdom
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