Difference between revisions of "Team:TCU Taiwan/Project/Overview"
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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 | [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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Revision as of 02:06, 20 August 2015
AMP. coli |
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.[1] Two kinds of AMPs were selected as our reagents: Epinecidin-1 and Signiferin.
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• Epinecidin-1: 1. From the skin mucus of Epinephelus coioides a kind of fish. 2. Has function of killing bacteria. 3. In addition, it has the ability to help wounds healing and has been proven by animal studies. • Signiferin: 1. From the skin mucus of Crinia signifera a kind of tree frog. 2. Have function of killing bacteria. 3. Have great ability in disinfect Methicillin-Resistant Staphylococcus aureus (MRSA). 4. Had already been kindly proved by the 2013 TU-Delft iGEM team. 1. Helps AMPs to secret out of E. coli. 2. From Streptomyces lividans to trasport chitinase C to secretion system, which has been proven to work in E.coli by reference. Based on AMPs to develop into a potential material of wound dressing. |
References
[1] Michael R. Yeaman & Nannette Y. Yount,..(2003) 'Mechanisms of Antimicrobial Peptide Action and Resistance' , Pharmacological Reviews,vol 55,p:27-55
[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.
[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.
[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
2-1-2, Tsukuba 305-8642, Japan Received 26 July 1999
[5] TAKESHI FUJII, KIYOTAKA MIYASHITA. Multiple domain structure in a chitinase gene (chic) of Streptomyces lividans. Journal of General Microbiology (1993), 139, 677-686
Contact us tcutaiwan@gmail.com No.701, Sec. 3, Zhongyang Rd. Hualien 97004, Taiwan |