Publication | Closed Access
A chemically-controlled supramolecular protein polymer formed by a myoglobin-based self-assembly system
55
Citations
32
References
2011
Year
Supramolecular AssemblyEngineeringFunctionalized Supramolecular PolymersMolecular Self-assemblyMolecular BiologyBiofabricationProtein FoldingSupramolecular Protein PolymerPrecision MacromoleculeBiophysicsPolymer ChemistryBiochemistryMyoglobin-based Self-assembly SystemMolecular EngineeringSupramolecular PolymerBiomolecular EngineeringNatural SciencesSelf-assemblyPolymer ScienceProtein EngineeringArtificial Self-assembling SystemsPolymer Self-assembly
Artificial self-assembling systems comprised of proteins have the potential not only for mimicking naturally occurring protein clusters but also for creating functionalized supramolecular polymers. Here we report a new type of a supramolecular protein polymer which utilizes the original character and reactivity of the monomer protein. Myoglobin, an oxygen storage hemoprotein, was chosen as the monomer unit and was provided with an externally-attached heme on the protein surface which drives the formation of the fibrous supramolecular assembly through successive interprotein interactions between the external heme and the protein matrix. This assembly governed by myoglobin characteristics shows chemically-responsive stability and can be converted into extremely large protein clustersvia cross-linking. Interestingly, the assembly retains the oxygen storage function. Our present system can be used for construction of smart nanobiomaterials using various hemoproteins.
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