Biomod/2014/ASU

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  • /

.project_box > img {

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  1. protocols, #polymers_protocols, #origami_protocols, #reaction_protocols, #nanocontainer_protocols, #imaging_protocols {
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  1. protocols .interlude, #polymers_protocols .interlude, #origami_protocols .interlude, #reaction_protocols .interlude, #nanocontainer_protocols .interlude, #imaging_protocols .interlude {
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</p><p> <section id="content"> <nav id = "main-nav"> <ul id="nav-primary" > <li class = "selected"><a href="http://openwetware.org/wiki/Biomod/2014/ASU"><i class="menu-icon icon-team"></i><span>Main</span></a></li> <li><a href="http://openwetware.org/wiki/Biomod/2014/ASU/Project"><i class="menu-icon icon-team"></i><span>Project</span></a></li> <li><a href="http://openwetware.org/wiki/Biomod/2014/ASU/Design"><i class="menu-icon icon-studio"></i><span>Design</span></a></li> <li><a href="#"><i class="menu-icon icon-studio"></i><span>Experiment</span></a>

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<li><a href="http://openwetware.org/wiki/Biomod/2014/ASU/Team"><i class="menu-icon icon-studio"></i><span>Team</span></a></li>

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<p style = "font-weight: bold; font-family: Times New Roman; color: #000000; font-size: 16px;"> Hello and welcome to our page! We are team NanoDevils from Arizona State University. This page is created to showcase our story leading up to Biomod. Below is an introductory video of our project. For more specific details, proceed to the rest of the tabs of this website for visuals, methods, results, and more! </p><br>

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<p style = "color: #000000; font-size: 16px;">Antibodies are one of the immune system’s most amazing tools for fighting pathogens. They are multivalent proteins, and they are the product of a recombinatory process, which gives them the potential to bind to a wide variety of different targets. Our goal is to use the power and flexibility of DNA nanotechnology to develop a multivalent binding surface that would mimic natural antibodies. We want to base such a structure on a DNA tile, or origami, in order to exploit the straightforward and reliable self-assembly process of these nanostructures. Therefore, we designed a tile that is able to host up to 4 binding sites (aptamers). The characterization of the tile binding properties is performed with a test target protein, human alpha-thrombin, and some aptamers known to bind to it. We then coordinate aptamers located at nearby sites on the DNA tile. What we would like to achieve as a result of the evolution process is a “DNA surface” with a quaternary structure that will possibly increase the range of conformations beyond what is achievable with single-stranded aptamers. We propose that the end product will show significantly enhanced affinity and selectivity for its target. In parallel to the experimental approach, we are setting up computational methods, including Molecular Dynamics simulations, to model and further understand the protein-tile interactions.</p> <br>

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