Difference between revisions of "Team:DTU-Denmark/Project/Overview"

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                  >Overview
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                <a href="/Team:DTU-Denmark/Project/Background"
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                  >Background
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                <a href="/Team:DTU-Denmark/Project/MAGE"
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                  >MAGE subtilis
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                  </a></li>
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                <a href="/Team:DTU-Denmark/Project/Tyrocidine"
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                  >Tyrocidine
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                  </a></li>
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                <a href="/Team:DTU-Denmark/Project/Chip"
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                  >Lab-on-a-disc
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                <a href="/Team:DTU-Denmark/Project/Inteins"
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                  >Inteins
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                <a href="/Team:DTU-Denmark/Project/Detection"
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                  >Detection of NRP
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                  <span class="caret"></span></a><ul class="dropdown-menu" role="menu">
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                  >Parts
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                  >Characterisation of xylR
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                  </a></li></ul></li>
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                  >Judging Form
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                  </a></li></ul></li>
 
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<p>Over the summer we worked with nonribosomal peptide synthetases (NRPSs). We developed a&nbsp;<em>B. subtilis</em>&nbsp;strain capable of oligo-mediated genome engineering and used this strain to alter a NRPS. We also investigated methods of screening for novel products with desired activities.</p>
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      Introduction
 +
    </h1>
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      <p>Over the summer we worked with nonribosomal peptide synthetases (NRPSs). We developed a&nbsp;<em>B. subtilis</em>&nbsp;strain capable of oligo-mediated genome engineering and used this strain to alter a NRPS. We also investigated methods of screening for novel products with desired activities.</p>
  
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<p>Nonribosomal peptide synthases (NRPSs) are large multimodular enzymes that synthesize nonribosomal peptides, which are short bioactive peptides with a broad range of functions, including antibiotics, immunosuppressants and anticancer drugs.</p>
+
      Background
 +
    </h1>
 +
      <p>Nonribosomal peptide synthases (NRPSs) are large multimodular enzymes that synthesize nonribosomal peptides, which are short bioactive peptides with a broad range of functions, including antibiotics, immunosuppressants and anticancer drugs.</p>
  
−
<div class="overview-readmore"><a href="/Team:DTU-Denmark/Project/Background">Read more</a></div>
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<p>Multiplex automated genome engineering (MAGE) utilises cyclical recombination with short oligonucleotides in order to achieve a high allelic replacement efficiency and can be used to quickly generate cell populations with varying phenotypes. We introduced oligo-mediated genome engineering into <i>Bacillus subtilis</i>.</p>
+
      MAGE subtilis
 +
    </h1>
 +
      <p>Multiplex automated genome engineering (MAGE) utilises cyclical recombination with short oligonucleotides in order to achieve a high allelic replacement efficiency and can be used to quickly generate cell populations with varying phenotypes. We introduced oligo-mediated genome engineering into <i>Bacillus subtilis&nbsp;</i>and used it to alter a nonribosomal peptide synthetase.</p>
  
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<p>In order to verify that we could alter specificities of nonribosomal peptide synthetases to produce novel compounds, we used oligo-mediated recombineering to alter the surfactin peptide of <i>B. subtilis</i>.</p>
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      <p>Tyrocidine is a mixture of non-ribosomal peptides. It can only be used topically due to its toxicity. We sought to express the tyrocidine synthase cluster in <i>B. subtilis</i>&nbsp;to make novel derivatives with oligo-mediated recombineering.</p>
  
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<p>Tyrocidine is a mixture of non-ribosomal peptides. It can only be used topically due to its toxicity. We sought to express the tyrocidine synthase cluster in <i>B. subtilis</i>&nbsp;to make novel derivatives with oligo-mediated recombineering.</p>
 
−
 
−
<div class="overview-readmore">
 
 
<p><a href="/Team:DTU-Denmark/Project/Tyrocidine">Read more</a></p>
 
<p><a href="/Team:DTU-Denmark/Project/Tyrocidine">Read more</a></p>
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      <p>Lab-on-a-disc is a potential&nbsp;screening method for our MAGE NRPS products. After screening for antimicrobial activity, prospective MAGE edited NRPS products could be tested for different beneficial properties. One example is a quick screening method for cytotoxicity.</p>
  
−
<div class="overview-readmore">
 
 
<p><a href="/Team:DTU-Denmark/Project/Chip">Read more</a></p>
 
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 +
    </h1>
 +
      <p>When one method fails the Synthesizer team has to innovate! We explored an alternative approach for generating short, cyclized peptides with similar length to tyrocidine by using self-splicing proteins. These&nbsp;short, self-splicing proteins that have no function&nbsp;in the proteins they are a part of, besides catalyzing&nbsp;their own&nbsp;excision after translation, are called inteins. The splicing creates a peptide bond between the two&nbsp;adjacent amino acids next to the inteins and we hypothesized that it could be used to make our cyclic peptides.</p>
  
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 +
    </h1>
 +
      <p>Separation and identification of our non-ribosomal peptide synthetase (NRPS) products was determined by ultra-high performance liquid chromatography with diode array detection coupled to quadrupole time-of-flight mass spectrometry (UHPLC-DAD-QTOFMS). NRPS variants were identified by changes in mass-to-charge ratio&nbsp;and column retention time.&nbsp;</p>
  
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Latest revision as of 14:34, 9 November 2015


Overview

Scroll down for more

Project

Introduction

Over the summer we worked with nonribosomal peptide synthetases (NRPSs). We developed a B. subtilis strain capable of oligo-mediated genome engineering and used this strain to alter a NRPS. We also investigated methods of screening for novel products with desired activities.

Background

Nonribosomal peptide synthases (NRPSs) are large multimodular enzymes that synthesize nonribosomal peptides, which are short bioactive peptides with a broad range of functions, including antibiotics, immunosuppressants and anticancer drugs.

Read more

MAGE subtilis

Multiplex automated genome engineering (MAGE) utilises cyclical recombination with short oligonucleotides in order to achieve a high allelic replacement efficiency and can be used to quickly generate cell populations with varying phenotypes. We introduced oligo-mediated genome engineering into Bacillus subtilis and used it to alter a nonribosomal peptide synthetase.

Read more

Tyrocidine

Tyrocidine is a mixture of non-ribosomal peptides. It can only be used topically due to its toxicity. We sought to express the tyrocidine synthase cluster in B. subtilis to make novel derivatives with oligo-mediated recombineering.

Read more

Lab-on-a-disc

Lab-on-a-disc is a potential screening method for our MAGE NRPS products. After screening for antimicrobial activity, prospective MAGE edited NRPS products could be tested for different beneficial properties. One example is a quick screening method for cytotoxicity.

Read more

Intein

When one method fails the Synthesizer team has to innovate! We explored an alternative approach for generating short, cyclized peptides with similar length to tyrocidine by using self-splicing proteins. These short, self-splicing proteins that have no function in the proteins they are a part of, besides catalyzing their own excision after translation, are called inteins. The splicing creates a peptide bond between the two adjacent amino acids next to the inteins and we hypothesized that it could be used to make our cyclic peptides.

Read more

NRP Detection

Separation and identification of our non-ribosomal peptide synthetase (NRPS) products was determined by ultra-high performance liquid chromatography with diode array detection coupled to quadrupole time-of-flight mass spectrometry (UHPLC-DAD-QTOFMS). NRPS variants were identified by changes in mass-to-charge ratio and column retention time. 

Read more

Technical University of Denmark
Department of Systems Biology
Søltofts Plads 221
2800 Kgs. Lyngby
Denmark
P: +45 45 25 25 25
M: dtu-igem-2015@googlegroups.com