"
Team:Arizona State/Magainin
From 2012.igem.org
| Line 17: | Line 17: | ||
<h2>Biosensor Design Concept</h2> | <h2>Biosensor Design Concept</h2> | ||
| + | |||
| + | [[Image:https://static.igem.org/mediawiki/2012/1/19/ASUiGEM2012_magaininconcept.png|200px]] | ||
<h2>Progress Map</h2> | <h2>Progress Map</h2> | ||
Revision as of 05:23, 3 October 2012
Magainin-Split Beta-Galactosidase Biosensor
Overview
Current methods of water-borne pathogen detection require expensive equipment that often isn't modular, high throughput, or accessible to developing countries. One of the projects this year's ASU iGEM undertook was building a split-enzyme engineered fusion protein consisting of the Magainin peptide and the split alpha and omega fragments of beta-galactosidase.
Magainin
Magainins are a class of proteins found in the skin of Xenopus laevis[http://en.wikipedia.org/wiki/Xenopus_laevis] - the African clawed frog - that contain antimicrobial properties. Both Magainin 1 and 2 are closely related peptides of 23 amino acids each and only differ by two amino acid substitutions. These two peptides have broad spectrum antimicrobial activity, including gram-positive and gram-negative bacteria, viruses, protozoa, yeasts and fungi, and are hemolytic and cytotoxic to cancer cells. The mechanism for antimicrobial activity in Magainin 1 and 2 involves the disruption the plasma membranes of target cells via electrostatic interactions between the negatively charged phospholipid bilayer and the positively-charged amino-terminus of the Magainin peptide.
The design of the biosensor took advantage of the electrostatic interaction between the Magainin-1 peptide and the lipid bilayer of bacteria to design a bacterial biosensor that confers a signal based on the binding of multiple Magainin peptides to a bacterial membrane.
