Difference between revisions of "Team:TCU Taiwan/Project/Our Design"

 
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                 <br>Antimicrobial peptide
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                 <br>Antimicrobial peptides
 
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Antibiotic is the method of choice to fight bacterial infection. However due to over use of antibiotics drug-resistant bacteria frequently appear. Making recovery difficult. Nowadays more and more focuses put on new infectious agents to fight with these pathogens.
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Antibiotic administration is the current method of choice to fight a bacterial infection. However, due to over-use of antibiotics, drug-resistant bacteria have emerged and frequently appear such as methicillin-resistant <I>Staphylocccus aureus</I> (MRSA). This complication makes decreases wound healing potential and makes recovery increasingly difficult. Currently, more focus has been placed on new anti-infectious agents to fight these drug-resistant pathogens.
 
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Antimicrobial peptides (AMPs) are stable peptides that have extensive ability to kill or inhibit the growth of bacteria. They play a role in defense mechanism for all organisms, ranging from prokaryotes to humans, to against predators. Some of them act against specific strain of microbes. Unlike antibiotics, AMPs use their chargeability to interact with bacteria cell membrane. Than use hydrophobic region interfere the membrane structure thus make the cell going to lysis process. <a href="#">[1]</a> And pass through bacterial antibiotic drug resistance mechanisms. Besides, AMPs play multiple functions in immune system. They have ability to alter the properties of mammalian cells and effect cellular process to help wound healing.<a href="#">[2]</a>
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Antimicrobial peptides (AMPs) are stable peptides that have extensive abilities to kill or inhibit the growth of bacteria. They play a role in defense mechanism for all organisms, ranging from prokaryotes to humans. Some peptides act against specific strains of microbes. Unlike antibiotics, AMPs use their chargeability to interact with bacteria cell membrane. Than use hydrophobic region interfere the membrane structure. This leads to cell lysis and bypasses bacterial antibiotic drug-resistance mechanisms. <a href="#tcu_amp_references_1">[1]</a> AMPs also functions in multiple roles in the immune system. Through target specificity, charge and bacterial toxicity, AMPs have the ability to alter the properties of mammalian cells and help in wound healing.<a href="#tcu_amp_references_2">[2]</a>
 
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The reasons why we choose these AMPs are because of their target specificity, charge, toxicity and their effect in healing process. We choose two kinds of AMPs: Signiferin and Epinecidin-1 as our reagents. Signiferin is a peptide came from the skin mucus of <I>Crinia signifera</I> (tree frog). It demonstrated effectiveness in killing MRSA, and had been kindly proved by the TU-Delft 2013 iGEM team.<a href="#">[3]</a> Epinecidin-1 is a peptide came from the skin mucus of <I>Epinephelus coioides</I>. It has ability to help wound healing and has been proven by animal studies, and was selected as an additional reagent.<a href="#">[4]</a>
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We choose two types of AMPs, Signiferin and Epinecidin-1, as our reagents. Signiferin is a peptide derived from the skin mucus of <I>Crinia signifera</I> (tree frog). It has demonstrated effectiveness in killing MRSA, and has been proven by the TU-Delft 2013 iGEM team.<a href="#tcu_amp_references_3">[3]</a> Epinecidin-1 is a peptide originating from the skin mucus of <I>Epinephelus coioides</I>.<a href="#tcu_amp_references_4">[4]</a> It has ability to help wound healing and has been proven by animal studies.<a href="#tcu_amp_references_5">[5]</a>
 
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     &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;Reference
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     References
 
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<td style="vertical-align:text-top;" align="left">[1]</td>
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Yeaman, M.R. and N.Y. Yount, <I>Mechanisms of antimicrobial peptide action and resistance</I>. Pharmacol Rev, 2003. 55(1): p. 27-55.
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<td style="vertical-align:text-top;" align="left">[2]</td>
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Lai, Y. and R.L. Gallo, AMPed up immunity: <I>how antimicrobial peptides have multiple roles in immune defense. Trends Immunol</I>, 2009. 30(3): p. 131-41.
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<td width="11%"style="vertical-align:text-top;" align="left" >[3]</td>
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TU_Delf, i.t. 2013; Available from: <a href="https://2013.igem.org/Team:TU-Delft">https://2013.igem.org/Team:TU-Delft</a>.
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<td style="vertical-align:text-top;" align="left">[4]</td>
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Huang, H.N., et al.,<I> Use of the antimicrobial peptide Epinecidin-1 to protect against MRSA infection in mice with skin injuries</I>. Biomaterials, 2013. 34(38): p. 10319-27
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<td style="vertical-align:text-top;" align="left">[5]</td>
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Pan, C.Y., et al., Gene expression and localization of the epinecidin-1 antimicrobial peptide in the grouper (Epinephelus coioides), and its role in protecting fish against pathogenic infection. DNA Cell Biol, 2007. 26(6): p. 403-13.
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Latest revision as of 15:02, 29 October 2015



Antimicrobial peptides

Antibiotic administration is the current method of choice to fight a bacterial infection. However, due to over-use of antibiotics, drug-resistant bacteria have emerged and frequently appear such as methicillin-resistant Staphylocccus aureus (MRSA). This complication makes decreases wound healing potential and makes recovery increasingly difficult. Currently, more focus has been placed on new anti-infectious agents to fight these drug-resistant pathogens.

Antimicrobial peptides (AMPs) are stable peptides that have extensive abilities to kill or inhibit the growth of bacteria. They play a role in defense mechanism for all organisms, ranging from prokaryotes to humans. Some peptides act against specific strains of microbes. Unlike antibiotics, AMPs use their chargeability to interact with bacteria cell membrane. Than use hydrophobic region interfere the membrane structure. This leads to cell lysis and bypasses bacterial antibiotic drug-resistance mechanisms. [1] AMPs also functions in multiple roles in the immune system. Through target specificity, charge and bacterial toxicity, AMPs have the ability to alter the properties of mammalian cells and help in wound healing.[2]

We choose two types of AMPs, Signiferin and Epinecidin-1, as our reagents. Signiferin is a peptide derived from the skin mucus of Crinia signifera (tree frog). It has demonstrated effectiveness in killing MRSA, and has been proven by the TU-Delft 2013 iGEM team.[3] Epinecidin-1 is a peptide originating from the skin mucus of Epinephelus coioides.[4] It has ability to help wound healing and has been proven by animal studies.[5]

References


[1] Yeaman, M.R. and N.Y. Yount, Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev, 2003. 55(1): p. 27-55.

[2] Lai, Y. and R.L. Gallo, AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol, 2009. 30(3): p. 131-41.

[3] TU_Delf, i.t. 2013; Available from: https://2013.igem.org/Team:TU-Delft.

[4] Huang, H.N., et al., Use of the antimicrobial peptide Epinecidin-1 to protect against MRSA infection in mice with skin injuries. Biomaterials, 2013. 34(38): p. 10319-27
[5] Pan, C.Y., et al., Gene expression and localization of the epinecidin-1 antimicrobial peptide in the grouper (Epinephelus coioides), and its role in protecting fish against pathogenic infection. DNA Cell Biol, 2007. 26(6): p. 403-13.





             
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