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• W2047082896 abstract "Programmed biomolecular self-assembly is a powerful method for the construction of designed supramolecular materials. Here, we show that branched ∼8 kDa subunits composed of α-helical coiled-coil protein domains cross-linked at their midpoints by an organic bridging group can form defined supramolecular polymer assemblies in aqueous solution. The subunits are accessible by a modular and convergent synthetic route based on the chemoselective ligation of unprotected peptide building blocks. Systematic characterization of solution folding and self-assembly demonstrate that the properties of the assemblies (e.g., chain length, hydrodynamic radius) are sensitive to both the structure of the organic bridge and the sequence of the protein domain. These findings raise the possibility of the rational design of a family of supramolecular materials with tunable properties based on well-established sequence–folding relationships in coiled-coil proteins." @default.
• W2047082896 created "2016-06-24" @default.
• W2047082896 creator A5018394081 @default.
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• W2047082896 date "2012-01-01" @default.
• W2047082896 modified "2023-10-11" @default.
• W2047082896 title "A modular synthetic platform for the construction of protein-based supramolecular polymers via coiled-coil self-assembly" @default.
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• W2047082896 doi "https://doi.org/10.1039/c2sc20729j" @default.
• W2047082896 hasPublicationYear "2012" @default.
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