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Team:Slovenia/Biobrick
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The goal of our project was to investigate and demonstrate the feasibility of polypeptide assembly based on modular nanoBricks. Potentials of this approach are vast (see Discussion and Vision) and for the development of applications it is essential to have available a large collection of “nuts and bolts” to assemble polypeptide nanostructures. We produced all together more than 100 BioBricks, which comprise a significant number of different natural as well as designed coiled-coil forming segments as well as different polypeptide oligomerization domains. In addition we prepared several “functional polypeptides”, which provide additional useful features to the material, such as different biological activities (antimicrobial peptide, growth factors, cell attachment motifs…), optical properties, enzymatic activity... | The goal of our project was to investigate and demonstrate the feasibility of polypeptide assembly based on modular nanoBricks. Potentials of this approach are vast (see Discussion and Vision) and for the development of applications it is essential to have available a large collection of “nuts and bolts” to assemble polypeptide nanostructures. We produced all together more than 100 BioBricks, which comprise a significant number of different natural as well as designed coiled-coil forming segments as well as different polypeptide oligomerization domains. In addition we prepared several “functional polypeptides”, which provide additional useful features to the material, such as different biological activities (antimicrobial peptide, growth factors, cell attachment motifs…), optical properties, enzymatic activity... | ||
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On the other hand we extended the BioBrick standard by introducing sites that allow extension of peptide linker sequences. Length of the linkers between polypeptide domains is crucial to determine the accessible geometry of the assembly, and our extended standard provides a tool to extend the length of a linker by any required length in increments of two residues. This task, particularly concerning small extensions would otherwise require the preparation of a new domain construct. | On the other hand we extended the BioBrick standard by introducing sites that allow extension of peptide linker sequences. Length of the linkers between polypeptide domains is crucial to determine the accessible geometry of the assembly, and our extended standard provides a tool to extend the length of a linker by any required length in increments of two residues. This task, particularly concerning small extensions would otherwise require the preparation of a new domain construct. | ||
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| + | For further information see: | ||
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| + | Development of BioBRICKs:<br> | ||
| + | [[Linker-extension standard]]<br> | ||
| + | [[nanoBRICKs[PRO]]] | ||
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| + | [[Deposited BioBRICKs]] | ||
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Revision as of 06:25, 21 October 2009
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bioBRICKSThe goal of our project was to investigate and demonstrate the feasibility of polypeptide assembly based on modular nanoBricks. Potentials of this approach are vast (see Discussion and Vision) and for the development of applications it is essential to have available a large collection of “nuts and bolts” to assemble polypeptide nanostructures. We produced all together more than 100 BioBricks, which comprise a significant number of different natural as well as designed coiled-coil forming segments as well as different polypeptide oligomerization domains. In addition we prepared several “functional polypeptides”, which provide additional useful features to the material, such as different biological activities (antimicrobial peptide, growth factors, cell attachment motifs…), optical properties, enzymatic activity...
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