Difference between revisions of "Team:GeorgiaTech/Description"
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| − | <h2> | + | <h2>Click Chemistry? So What?</h2> |
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| − | The copper-catalyzed azide-alkyne cycloaddition (<a href = | + | The copper-catalyzed azide-alkyne cycloaddition (<a href = "https://2015.igem.org/Team:GeorgiaTech/Background">CuAAC</a>) reaction has been widely used in the laboratory for tagging or labeling biological molecules (Hong, 2010), but it cannot be directly applied in living organisms because of the toxicity associated with excess or free copper ions (Biaglow, 1997). The development of an enzyme to catalyze the CuAAC reaction would perfectly complement the growing ability of scientists to introduce azide- and alkyne-labeled molecules into biological systems (Liu, 1999). Our goal is to discover a protein to bind Cu ions safely <i>in vivo</i> and perform the CuAAC reaction through an innovative approach. We will attempt this by <a href ="https://2015.igem.org/Team:GeorgiaTech/Background#library">generating a large library</a> of Cu-binding proteins. Later teams will develop a reliable <a href = "https://2015.igem.org/Team:GeorgiaTech/Background#phage">phage display</a> system to screen for the desired CuAAC activity, and evolving any active enzymes for improved function. |
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| − | "https://2015.igem.org/Team:GeorgiaTech/Background">CuAAC</a>) reaction | + | |
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| − | has been widely used in the laboratory for tagging or labeling | + | |
| − | + | ||
| − | biological molecules (Hong, 2010), but it cannot be directly applied | + | |
| − | + | ||
| − | in living organisms because of the toxicity associated with excess or | + | |
| − | + | ||
| − | free copper ions (Biaglow, 1997). The development of an enzyme to | + | |
| − | + | ||
| − | catalyze the CuAAC reaction would perfectly complement the growing | + | |
| − | + | ||
| − | ability of scientists to introduce azide- and alkyne-labeled molecules | + | |
| − | + | ||
| − | into biological systems (Liu, 1999). Our goal is to discover a protein | + | |
| − | + | ||
| − | to bind Cu ions safely <i>in vivo</i> and perform the CuAAC reaction | + | |
| − | + | ||
| − | through an innovative approach. We will attempt this by <a href | + | |
| − | + | ||
| − | ="https://2015.igem.org/Team:GeorgiaTech/Background#library">generating | + | |
| − | + | ||
| − | a large library</a> of Cu-binding proteins. Later teams will develop a | + | |
| − | + | ||
| − | reliable <a href = | + | |
| − | + | ||
| − | "https://2015.igem.org/Team:GeorgiaTech/Background#phage">phage | + | |
| − | + | ||
| − | display</a> system to screen for the desired CuAAC activity, and | + | |
| − | + | ||
| − | evolving any active enzymes for improved function. | + | |
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<h4>Bibliography</h4> | <h4>Bibliography</h4> | ||
| − | <ol><li>Biaglow, J. E.; Manevich, Y.; Uckun, F.; Held, K. D. <i>Free | + | <ol><li>Biaglow, J. E.; Manevich, Y.; Uckun, F.; Held, K. D. <i>Free Radic Biol Med</i> 1997, 22, 1129.</li> |
| − | + | <li>Hong, V.; Steinmetz, N. F.; Manchester, M.; Finn, M. G. <i>Bioconjug Chem</i> 2010, 21, 1912.</li> | |
| − | Radic Biol Med</i> 1997, 22, 1129.</li> | + | <li>Liu, D. R.; Schultz, P. G. <i>Proc Natl Acad Sci U S A</i> 1999, 96, 4780.</li></ol> |
| − | <li>Hong, V.; Steinmetz, N. F.; Manchester, M.; Finn, M. G. | + | |
| − | + | ||
| − | <i>Bioconjug Chem</i> 2010, 21, 1912.</li> | + | |
| − | <li>Liu, D. R.; Schultz, P. G. <i>Proc Natl Acad Sci U S A</i> 1999, | + | |
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| − | 96, 4780.</li></ol> | + | |
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Revision as of 21:30, 18 September 2015
Click Chemistry? So What?
The copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction has been widely used in the laboratory for tagging or labeling biological molecules (Hong, 2010), but it cannot be directly applied in living organisms because of the toxicity associated with excess or free copper ions (Biaglow, 1997). The development of an enzyme to catalyze the CuAAC reaction would perfectly complement the growing ability of scientists to introduce azide- and alkyne-labeled molecules into biological systems (Liu, 1999). Our goal is to discover a protein to bind Cu ions safely in vivo and perform the CuAAC reaction through an innovative approach. We will attempt this by generating a large library of Cu-binding proteins. Later teams will develop a reliable phage display system to screen for the desired CuAAC activity, and evolving any active enzymes for improved function.
Bibliography
- Biaglow, J. E.; Manevich, Y.; Uckun, F.; Held, K. D. Free Radic Biol Med 1997, 22, 1129.
- Hong, V.; Steinmetz, N. F.; Manchester, M.; Finn, M. G. Bioconjug Chem 2010, 21, 1912.
- Liu, D. R.; Schultz, P. G. Proc Natl Acad Sci U S A 1999, 96, 4780.