Difference between revisions of "Team:TU Darmstadt/project/chemistry"

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<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project" class="active">Project</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project" class="active">Project</a></li>
 
                                         <div class="nav-proj-drop">
 
                                         <div class="nav-proj-drop">
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<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/chitin_synthase">Chitin Synthase</a></li>
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<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/chitin_synthase">Chitin synthase</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/chitinase">Chitinase</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/chitinase">Chitinase</a></li>
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<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/chitin_deacetylase">Chitin Deacetylase</a></li>
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<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/chitin_deacetylase">Chitin deacetylase</a></li>
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<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/regulation_system">Regulation System</a></li>
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<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/regulation_system">Regulation system</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/chemistry" class="active">Chemistry</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/chemistry" class="active">Chemistry</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/modeling">Modeling</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/project/modeling">Modeling</a></li>
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                                         <div class="nav-drop">
 
                                         <div class="nav-drop">
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/human_practices">Human Practices</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/human_practices">Human Practices</a></li>
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<li><a href="https://2017.igem.org/Team:TU_Darmstadt/tech">Tech</a></li>
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<li><a href="https://2017.igem.org/Team:TU_Darmstadt/hardware">Hardware</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/team">Team</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/team">Team</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/judging">Judging</a></li>
 
<li><a href="https://2017.igem.org/Team:TU_Darmstadt/judging">Judging</a></li>
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         <div class="container">
 
         <div class="container">
 
<header class="major">
 
<header class="major">
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<h2>The Project: ChiTUcare</h2><!--BIG HEADING-->
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<h2>Chemical modification of Chitosan for the use in protease-sensing wound coatings.</h2><!--BIG HEADING-->
 
</header>
 
</header>
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<p>Abstract: Faucibus sed lobortis aliquam lorem blandit. Lorem eu nunc metus col. Commodo id in arcu ante lorem ipsum sed accumsan erat praesent faucibus commodo ac mi lacus. Adipiscing mi ac commodo. Vis aliquet tortor ultricies non ante erat nunc integer eu ante ornare amet commetus vestibulum blandit integer in curae ac faucibus integer non. Adipiscing cubilia elementum.</p>
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<h3>Abstract</h3>
 +
<p>
 +
Chitosan, especially a chitosan-based hydrogel, can be modified at the amino group with succinyl anhydride and a variable Peptide with a fluorogenic substrate
 +
to form a reliable system to detect proteases. In this study, we reproduce the findings of the Paper “Enzyme-Sensing Chitosan Hydrogels” by Mir Morteza Sadat Ebrahimi
 +
and Holger Schönherr from the university of Siegen and use the fluorogenic substrate alanyl-alanyl-phenylalanine-7-amido-4-methylcoumarin (AAP-AMC) to detect
 +
α-chymotrysin.
 +
This protease is secreted by Staphylococcus aureus or Pseudomonas aeruginosa, which are examples of pathogenic bacteria that can infect wounds.
 +
</p>
 
</div>
 
</div>
 
</section>
 
</section>
 
<section id="two"><div class="container">
 
<section id="two"><div class="container">
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<h3>Submenu 1 id "two"</h3>
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<h3>Introduction</h3>
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<p>Abstract: Faucibus sed lobortis aliquam lorem blandit. Lorem eu nunc metus col. Commodo id in arcu ante lorem ipsum sed accumsan erat praesent faucibus commodo ac mi lacus. Adipiscing mi ac commodo. Vis aliquet tortor ultricies non ante erat nunc integer eu ante ornare amet commetus vestibulum blandit integer in curae ac faucibus integer non. Adipiscing cubilia elementum.</p>
+
<p>
 +
Badly healing wounds are still a big issue in clinical medicine all over the world. Especially inflamed wounds often exhibit impaired healing properties and are prone
 +
to infections of opportunistic pathogenic bacteria. On the one hand, wounds have to be screened for infections extensively, on the other hand, they have to be kept wet
 +
and in an Oxygen-free atmosphere for optimal healing conditions. Thus there is an obvious contradiction between the best healing conditions and the commonly
 +
used
 +
infection swab test, where you have to remove the wound coating. Furthermore, current swab tests needs a few days to evaluate the presence of pathogenic bacteria,
 +
but it is important to get this information as soon as possible and to start the suitable treatment.
 +
Ebrahimi and Schönherr developed a quick and non invasive detection
 +
method for wound infections without the necessity to remove the wound coating. The principle of the test is the modification of an amino group of chitosan with
 +
succinic anhydride to gain a carboxyl group that can be linked to the amino group of our alanyl-alanyl-phenylalanine peptide linker.
 +
This peptide linker is fused to
 +
our actual detectable unit, the methylcoumarin.</p>
 +
<img src="https://static.igem.org/mediawiki/2017/4/4a/T--TU_Darmstadt--Flourophor_linken.jpg" />
 +
<p>This linker was chosen due to the fact that chymotrysin cleaves peptides n-terminal of aromatic amino acids.</p>
 +
<img src="https://static.igem.org/mediawiki/2017/2/25/T--TU_Darmstadt--cleavedge.jpg" />
 +
<p>In our studies, we present an uncomplicated method to repeat the work of Ebrahimi and Schönherr in a way that works for iGEMers and FabLabers.  
 +
For that, we combined a few instructions to guarantee a working product without the need of expensive instrumental analysis.</p>
 
</div>
 
</div>
 
     </section>
 
     </section>

Revision as of 18:04, 13 October 2017

MainPage

Chemical modification of Chitosan for the use in protease-sensing wound coatings.

Abstract

Chitosan, especially a chitosan-based hydrogel, can be modified at the amino group with succinyl anhydride and a variable Peptide with a fluorogenic substrate to form a reliable system to detect proteases. In this study, we reproduce the findings of the Paper “Enzyme-Sensing Chitosan Hydrogels” by Mir Morteza Sadat Ebrahimi and Holger Schönherr from the university of Siegen and use the fluorogenic substrate alanyl-alanyl-phenylalanine-7-amido-4-methylcoumarin (AAP-AMC) to detect α-chymotrysin. This protease is secreted by Staphylococcus aureus or Pseudomonas aeruginosa, which are examples of pathogenic bacteria that can infect wounds.

Introduction

Badly healing wounds are still a big issue in clinical medicine all over the world. Especially inflamed wounds often exhibit impaired healing properties and are prone to infections of opportunistic pathogenic bacteria. On the one hand, wounds have to be screened for infections extensively, on the other hand, they have to be kept wet and in an Oxygen-free atmosphere for optimal healing conditions. Thus there is an obvious contradiction between the best healing conditions and the commonly used infection swab test, where you have to remove the wound coating. Furthermore, current swab tests needs a few days to evaluate the presence of pathogenic bacteria, but it is important to get this information as soon as possible and to start the suitable treatment. Ebrahimi and Schönherr developed a quick and non invasive detection method for wound infections without the necessity to remove the wound coating. The principle of the test is the modification of an amino group of chitosan with succinic anhydride to gain a carboxyl group that can be linked to the amino group of our alanyl-alanyl-phenylalanine peptide linker. This peptide linker is fused to our actual detectable unit, the methylcoumarin.

This linker was chosen due to the fact that chymotrysin cleaves peptides n-terminal of aromatic amino acids.

In our studies, we present an uncomplicated method to repeat the work of Ebrahimi and Schönherr in a way that works for iGEMers and FabLabers. For that, we combined a few instructions to guarantee a working product without the need of expensive instrumental analysis.