Self-assembling membranes Idea Approach.html
From 2009.igem.org
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+ | =Self-assembling polypeptide membranes with adjustable pore properties= | ||
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We investigated potentials of fusing protein oligomerization domain with coiled-coil-forming domain for the formation of nanostructures. This combination should form a two- or three-dimensional lattice if the coiled-coil-forming domain forms an antiparallel homodimer. Particular advantage of this approach is that we can incrementally extend or modify the coiled coil-forming domain, which results in modification of the size of the lattice unit as well as in the size of pores enclosed by coiled-coil segments. | We investigated potentials of fusing protein oligomerization domain with coiled-coil-forming domain for the formation of nanostructures. This combination should form a two- or three-dimensional lattice if the coiled-coil-forming domain forms an antiparallel homodimer. Particular advantage of this approach is that we can incrementally extend or modify the coiled coil-forming domain, which results in modification of the size of the lattice unit as well as in the size of pores enclosed by coiled-coil segments. | ||
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- | We designed and prepared fusion protein between p53 tetramerization domain and antiparallel coiled-coil domain. This type of nanomaterial contains nanopores of defined size, which could be used to separate molecules or molecular assemblies according to their size. We assembled the material by a refolding procedure and tested it in a real world application as ultrafiltration membrane. The membranes efficiently remove large molecules and viruses from the sample. | + | We designed and prepared fusion protein between p53 tetramerization domain and a homodimeric antiparallel coiled-coil domain. This type of nanomaterial contains nanopores of defined size, which could be used to separate molecules or molecular assemblies according to their size. We assembled the material by a refolding procedure and tested it in a real world application as ultrafiltration membrane. The membranes efficiently remove large molecules and viruses from the sample. |
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<center> <img src="https://static.igem.org/mediawiki/2009/b/b8/Protein_membranes_summary_fig1.GIF" width="596" height="473" border="0" /> | <center> <img src="https://static.igem.org/mediawiki/2009/b/b8/Protein_membranes_summary_fig1.GIF" width="596" height="473" border="0" /> | ||
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- | <b>Figure 1:</b> The self-assembled polypeptide membrane and its | + | <b>Figure 1:</b> The summary of the idea of self-assembled polypeptide membrane and its performance in removing viruses from solution. A) The polypeptide material composed of tetramerization domain linked to coiled-coil-forming domain . B) The removal of viruses from the solution with the self-assembled polypeptide membrane. |
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<b>Figure 3:</b> Scheme of the constructs (A) and 3D model of APH-p53 fusion construct (B). | <b>Figure 3:</b> Scheme of the constructs (A) and 3D model of APH-p53 fusion construct (B). | ||
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+ | <li><a href="https://2009.igem.org/Self-assembling_membranes_Results.html" class="plavo">Results</a></li> | ||
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Latest revision as of 03:12, 22 October 2009
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Self-assembling polypeptide membranes with adjustable pore properties
Figure 1: The summary of the idea of self-assembled polypeptide membrane and its performance in removing viruses from solution. A) The polypeptide material composed of tetramerization domain linked to coiled-coil-forming domain . B) The removal of viruses from the solution with the self-assembled polypeptide membrane. The idea and approach
Figure 2: Assembly of a polypeptide consisting of a tetramerization domain and antiparallel homodimeric coiled-coil-forming domain results in a lattice with pores (circles) of defined size and properties depending on the nature of the coiled-coil segment. In order to test the formation and applicability of such designed membranes we prepared fusion proteins where oligomerization-prone domain is a tetramerization domain of p53 and a coiled-coil-forming segment is either a designed antiparallel homodimeric coiled-coil APH, APH1 (Gurnon, 2003) or BCR, a coiled-coil forming domain from the natural protein (Taylor, 2005). All of selected coiled-coil-forming domains associate into antiparallel coiled-coil dimers but they differ in length (45, 31 or 36 amino acid residues) and stability (Figure 3). We demonstrate that membranes formed by self-assembly of nanoBricks successfully retained large molecules and viruses when filtration was performed
Figure 3: Scheme of the constructs (A) and 3D model of APH-p53 fusion construct (B).
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