Difference between revisions of "Team:LMU-TUM Munich/Linkerchemistry"
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| + | Any cell mesh produced based on our bioink will suffer from exposition to serum-containing media or, in the case of in vivo application, the patient’s body fluids because of biotinidase. This ubiquitous enzyme is able to cleave biotin off of lysine -- at a lower rate also off of intact protein. We may now shift this hydrolysis in two directions: either to prevent it altogether and thus stabilize our cell mesh, or to accelerate it to make our mesh quickly disintegrable. To this end, we must consider how biotin is linked to the proteins in our bioink. | ||
| + | ==NHS Esters as Amine Coupling Reagents== | ||
=Design= | =Design= | ||
Revision as of 05:44, 10 October 2016
Introduction
Kopiervorlagen
Seitenverantwortliche/r:Vivien
References
Literaturreferenz[1]
Bei Google Scholar bitte das APA-Ziteirformat verwenden.
Textformatierung
kursiv
fett
Strich
Links
Wikiinterner Link Team:LMU-TUM_Munich/Materials (As described in the Materials section)
Wikiexterner Link Visit W3Schools
Visit W3Schools
Bilder
Introduction
Purpose
Any cell mesh produced based on our bioink will suffer from exposition to serum-containing media or, in the case of in vivo application, the patient’s body fluids because of biotinidase. This ubiquitous enzyme is able to cleave biotin off of lysine -- at a lower rate also off of intact protein. We may now shift this hydrolysis in two directions: either to prevent it altogether and thus stabilize our cell mesh, or to accelerate it to make our mesh quickly disintegrable. To this end, we must consider how biotin is linked to the proteins in our bioink.
NHS Esters as Amine Coupling Reagents
Design
Experiments
Proof of concept
Demonstrate
Discussion
References
- ↑ Schmidt, T. G., & Skerra, A. (2007). The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nature protocols, 2(6), 1528-1535.
