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| − | {{TCU_Taiwan/CSS}}
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| − | <html>
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| − | <style type="text/css">
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| − | #form {
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| − | </style>
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| − | <body>
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| − | <img src="https://static.igem.org/mediawiki/2015/5/5f/2015tcutaiwanProject.jpg" width="100%" align="center" />
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| − | <div id="form" style="background: rgba(100%,100%,100%,0.5); overflow-x:hidden;overflow-y:hidden; ">
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| − | <h1>
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| − | <table width="97%" align="center">
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| − | <span style="font-family:Arial Black;;line-height: 150%;">
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| − | <font size="8"><font-weight: 900;>
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| − | <br>AMP. <I>coli</I>
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| − | <table width="97%" align="center">
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| − | <p align="justify" ><span style="font-family:Calibri;line-height: 150%;"><font size="5">
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| − | Antimicrobial peptide (AMPs) has an extensive ability in disinfect. Unlike antibiotics, AMPs use chargeability puncture the cell membrane to kill the bacteria therefore by passing bacterial antibiotic drug resistance mechanisms. [1] Two kinds of AMPs were selected as our reagents: Epinecidin-1 and Signiferin. </br>
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| − | Epinecidin-1 is a peptide comes from <I>Epinephelus coioides</I>, and Signiferin is comes from <I>Crinia signifera</I>. Both of them are extracted from the skin mucus. In addition, epinecidin-1 has the ability to help wounds healing and has been proven by animal studies. [2] Moreover, signiferin have great ability in disinfect Methicillin-Resistant <I>Staphylococcus aureus</I> (S. aureus), and had already been kindly proved by the TU-Delft 2013 iGEM team. [3]Combining these two properties, we believe that can alleviate the serious problem of skin injury.</br>
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| − | To produce AMPs and control AMPs expression, we apply the Lac operon and ligate the DNA of signal peptide into E. <I>coli</I> to help AMPs secret into culture medium. [4][5] Next, to prove that AMPs have the extensive ability in disinfection and helps the wound healing, selected cells and bacteria were tested <I>in vitro</I>, including the squamous epithelial cell and endothelial cell of the blood vessel and MRSA, and mice were used <I>in vivo</I>. Ultimately, create a wound dressing based on the above procedure.</br>
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| − | An excellent dressing made of AMPs will make a fast recovery.</br>
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| − | </h1>
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| − | </div>
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| − | <div id="form" style="background: rgba(100%,100%,100%,0.5); overflow-x:hidden;overflow-y:hidden; ">
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| − | <p align="center">
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| − | <img align="middle" src="https://static.igem.org/mediawiki/2015/f/f0/Tcu_Taiwan_Project_overview.jpg" width=100% height=100% >
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| − | </p></div>
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| − | <div id="form" style="background: rgba(100%,100%,100%,0.5); overflow-x:hidden;overflow-y:hidden; ">
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| − | <table width="97%" align="center">
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| − | <tr>
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| − | <td width="3%"></td>
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| − | <td>
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| − | <span style="font-family:Calibri;line-height: 150%;text-align:justify;"><font size="5">
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| − | <p>
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| − | <a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Our_Design">
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| − | Antimicrobial peptide
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| − | </a>
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| − | </p>
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| − | <p align="justify">• Epinecidin-1:</p>
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| − | <p align="justify">1. From the skin mucus of <I>Epinephelus coioides</I> a kind of fish.
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| − | </p>
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| − | 2. Has function of killing bacteria.
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| − | </p>
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| − | <p align="justify">
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| − | 3. In addition, it has the ability to help wounds healing and has been proven by animal studies.
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| − | </p>
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| − | <br>
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| − | <p align="justify">• Signiferin:
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| − | </p>
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| − | <p align="justify">
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| − | 1. From the skin mucus of <I>Crinia signifera</I> a kind of tree frog.
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| − | </p>
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| − | <p align="justify">
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| − | 2. Have function of killing bacteria.
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| − | </p>
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| − | <p align="justify">
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| − | 3. Have great ability in disinfect Methicillin-Resistant <I>Staphylococcus aureus</I> (MRSA).
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| − | </p>
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| − | <p align="justify">
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| − | 4. Had already been kindly proved by the 2013 TU-Delft iGEM team.
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| − | </p>
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| − | <br>
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| − | <p>
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| − | <a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Experimental">Signal peptide: </a>
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| − | </p>
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| − | <p align="justify">
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| − | 1. Helps AMPs to secret out of E. coli.
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| − | </p>
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| − | <p align="justify">
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| − | 2. From <I>Streptomyces lividans</I> to trasport chitinase C to secretion system, which has been proven to work in E.<I>coli</I>
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| − | </p>
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| − | <p align="justify">
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| − | by reference.
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| − | </p>
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| − | <p style="font-size:0.7cm" align="justify">
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| − | <a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Reference">Wound dressing:</a>
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| − | <p align="justify">
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| − | Based on AMPs to develop into a potential material of wound dressing.
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| − | </p>
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| − | </font>
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| − | </span>
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| − | </td>
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| − | <td width="3%"></td>
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| − | </tr>
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| − | </table>
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| − | </div>
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| − | <a name="tcu_references_1"></a>
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| − | <div id="form" style="background: rgba(100%,100%,100%,0.5); overflow-x:hidden;overflow-y:hidden; ">
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| − | <table width="97%" align="center">
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| − | <span style="font-family:Calibri;line-height: 150%;text-align:justify;"><font size="5">
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| − | <p style="font-size:1.2cm" align="center">
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| − | References
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| − | <p style="font-size:0.6cm" align="justify">
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| − | <a name="tcu_references_2"></a>
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| − | <table width="100%" align="center" style="background-color: rgba(100%,100%,100%,0);line-height: 33px;">
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| − | <td width="5%">[1]</td>
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| − | <td width="90%">
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| − | Lai Y, Gallo RL. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 2009 Mar; 30(3):131-41. doi: 10.1016/j.it.2008.12.003. Epub 2009 Feb 13.
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| − | </td>
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| − | </tr>
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| − | </table>
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| − | <br>
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| − | <a name="tcu_references_3"></a>
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| − | <table width="100%" align="center" style="background-color: rgba(100%,100%,100%,0);line-height: 33px;">
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| − | <td width="5%">[2]</td>
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| − | Huang HN, Rajanbabu V, Pan CY, Chan YL, Wu CJ, Chen JY. Use of the antimicrobial peptide Epinecidin-1 to protect against MRSA infection in mice with skin injuries. Biomaterials. 2013 Dec; 34(38):10319-27. doi: 10.1016/j.biomaterials.2013.09.037. Epub 2013 Sep 27.
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| − | </td>
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| − | </tr>
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| − | </table>
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| − | <br>
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| − | <a name="tcu_references_4"></a>
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| − | <table width="100%" align="center" style="background-color: rgba(100%,100%,100%,0);line-height: 33px;">
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| − | <td width="5%">[3]</td>
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| − | <td width="90%">
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| − | Maselli VM, Bilusich D, Bowie JH, Tyler MJ. Host-defence skin peptides of the Australian Streambank Froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry. Rapid Commun Mass Spectrom. 2006; 20(5):797-803.
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| − | </td>
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| − | </tr>
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| − | </table>
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| − | <br>
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| − | <a name="tcu_references_5"></a>
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| − | <table width="100%" align="center" style="background-color: rgba(100%,100%,100%,0);line-height: 33px;">
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| − | <td width="5%">[4]</td>
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| − | <td width="90%">
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| − | Tokuyasu K, Kaneko S, Hayashi K, Mori Y. Production of a recombinant chitin deacetylase in the culture medium of Escherichia coli cells. FEBS Lett. 1999 Sep 10; 458(1):23-6.
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| − | </td>
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| − | </tr>
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| − | </table>
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| − | <br>
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| − | <table width="100%" align="center" style="background-color: rgba(100%,100%,100%,0);line-height: 33px;">
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| − | <td width="5%">[5]</td>
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| − | Fujii T, Miyashita K. Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans. J Gen Microbiol. 1993 Apr; 139(4):677-86.
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| − | </td>
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| − | </div>
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| − | <br><br><br><br><br>
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| − | </body>
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| − | </html>
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| − | {{TCU_Taiwan/CSSfooter}}
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