Team:TU Eindhoven/ZAP

From 2014.igem.org

(Difference between revisions)
Line 29: Line 29:
<div class="wrap">
<div class="wrap">
<div class="top">
<div class="top">
-
<h2>Zwitterionic Anitfouling Protein</h2>
+
<h2>Zwitterionic Antifouling Protein</h2>
  </div>
  </div>
</div>
</div>

Revision as of 15:12, 14 September 2014

Project Description

Zwitterionic Antifouling Protein

Introduction

A side project of this year’s TU Eindhoven iGEM Project is the Zwitterionic Encapsulation of a bacterial cell. The ultimate goal is however the same; create an antifouling encapsulation in order to evade the immune system. The difference is, however, that this approach encompasses a fully assembled system. Thus no alterations are possible as is the case with the click reaction. Roughly, the TU Eindhoven’s zwitterionic encapsulation is the result of zwitterionic interactions of polymers consisting of mainly Glutamic Acid (negatively charged) and Lysine (positively charged). We have chosen for these amino acids due to the demonstrated antifouling properties of the combination of these negatively and positively charged amino acids. [1]

The idea is therefore a polymer chain consisting of mainly Glutamic Acid and Lysine, bound to an anchor in order to facilitate the encapsulation around the bacterial cell. Penn iGEM team 2012 used an anchor which was able to bear a mCherry fluorescent group. Thus, the general idea is a bacterial cell littered with transmembrane anchors provided with a polymer chain comprising Glutamic Acids and Lysines. The amino acids interact with each other in order to form a network which is impervious for antibodies.



Bibliography

[1] Yang, Q., Wang, L., Lin, W., Ma, G., Yuan, J., & Chen, S. (2014). Development of nonfouling polypeptides with uniform alternating charges by polycondensation of the covalently bonded dimer of glutamic acid and lysine. Journal of Materials Chemistry B, 2, 577-584.