Difference between revisions of "Team:TCU Taiwan/Project/Overview"

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                <br>AMP. <I>coli</I>
 
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<p align="justify" ><span style="font-family:Calibri;line-height: 150%;"><font size="5">
 
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>
 
      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>
 
      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>
 
      An excellent dressing made of AMPs will make a fast recovery.</br>
 
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    <a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Our_Design">
 
            &nbsp;&nbsp;Antimicrobial peptide
 
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<p align="justify">&bull;&nbsp;Epinecidin-1:</p>
 
 
<p align="justify">1. From the skin mucus of <I>Epinephelus coioides</I> a kind of fish.
 
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2. Has function of killing bacteria.
 
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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 align="justify">&bull;&nbsp; Signiferin:
 
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1. From the skin mucus of <I>Crinia signifera</I> a kind of tree frog.
 
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2. Have function of killing bacteria.
 
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3. Have great ability in disinfect Methicillin-Resistant <I>Staphylococcus aureus</I> (MRSA).
 
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4. Had already been kindly proved by the 2013 TU-Delft iGEM team.
 
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<a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Experimental">Signal peptide: </a>
 
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1. Helps AMPs to secret out of E. coli.
 
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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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by reference.
 
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<a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Reference">Wound dressing:</a>
 
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Based on AMPs to develop into a potential material of wound dressing. 
 
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    References
 
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<td width="5%">[1]</td>
 
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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 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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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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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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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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Latest revision as of 05:33, 4 September 2015