The primary sequence control of polymers synthesized in biological systems is well beyond the capability of even the most sophisticated synthetic techniques.  It is the sequence that determines how biological molecules, such as proteins, fold and assemble into complex, functional hierarchical species.  Nevertheless, modern solid-phase microwave synthesis in combination with chromatographic techniques are capable of rapid production of peptides with excellent sequence fidelity.  Guided by theory and computational models, these peptides can be designed to fold and assemble into well-defined modular, coiled-coil bundles.  The enhanced stability of these bundles enables significant modulation of the functional groups at the periphery, creating a macromolecular unit with exact display of chemistry, which we establish as a fundamental building block for materials design and fabrication. <br/> <br/>Here, we implement computational modeling to generate non-biological peptide sequences that assemble into coiled-coil bundles.  Site-specific functionalization enables polymerization of these macromonomer units or ‘bundlemers.’   Polymers are synthesized using two bundlemers possessing complementary click functional groups.  A copolymerization of bundlemers with one-to-one stoichiometry yields large molecular weight polymers (&gt;1M g/mol) with persistence lengths in the 10s of microns.  Copolymerization of bundlemers with small molecular weight monomers and large molecular weight polymers produces flexible chains and crosslinked hydrogels, respectively.  Finally, the reversible nature of the bundle assemblies is further exploited to produce dynamic stimuli responsive materials.

Bundlemer polymerization: A peptide-based macromonomer approach to hierarchical materials synthesis

256th National Meeting (2018)

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