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">
 
AMPs have 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.<a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Overview#tcu_references_1">[1]</a> Two kinds of AMPs were selected as our reagents: Epinecidin-1 and Signiferin.
 
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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.<a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Overview#tcu_references_2">[2]</a> Moreover, signiferin have great ability in disinfect Methicillin-Resistant <I>Staphylococcus aureus</I> (<I>S. aureus</I>), and had already been kindly proved by the TU-Delft 2013 iGEM team. <a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Overview#tcu_references_3">[3]</a>Combining these two properties, we believe that can alleviate the serious problem of skin injury.
 
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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. <a href="https://2015.igem.org/Team:TCU_Taiwan/Project/Overview#tcu_references_4">[4][5]</a>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.
 
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An excellent dressing made of AMPs will make a fast recovery.
 
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            &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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[1] Michael R. Yeaman & Nannette Y. Yount,..(2003) 'Mechanisms of Antimicrobial Peptide Action and Resistance' , Pharmacological Reviews,vol 55,p:27-55
 
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[2] Han-Ning Huang, Chang-Jer Wu, Jyh-Yih Chen, Venugopal Rajanbabu , Chieh-Yu Pan, Yi-Lin Chan. Use of the antimicrobial peptide Epinecidin-1 to protect against MRSA infection in mice with skin injuries. Biomaterials 34 (2013) 10319e10327.
 
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<a name="tcu_references_4"></a>
 
[3] V.M. Maselli, D. Bilusich, et al., Host-defence skin peptides of the Australian Streambank Froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry, Rapid Communications in Mass Spectrometry, Volume 20, Issue 5, pages 797–803, Mar 2006.
 
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<a name="tcu_references_5"></a>
 
[4] Ken Tokuyasu, Satoshi Kaneko, Kiyoshi Hayashi, Yutaka Mori.Production of a recombinant chitin deacetylase in the culture medium of Escherichia coli cells.National Food Research Institute, Kannondai<br>2-1-2, Tsukuba 305-8642, Japan Received 26 July 1999
 
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[5] TAKESHI FUJII, KIYOTAKA MIYASHITA. Multiple domain structure in a chitinase gene (chic) of Streptomyces lividans. Journal of General Microbiology (1993), 139, 677-686
 
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Latest revision as of 05:33, 4 September 2015