Nature uses proteins and nucleic acids to form a wide array of functional architectures, and scientists have found inspiration from these structures in the rational design of synthetic biomaterials. We have recently shown that a modular subunit consisting of two alpha-helical coiled coil peptides attached at their midpoints by an organic linking group can spontaneously self-assemble in aqueous solution to form a soluble supramolecular polymer. Here we explore the use of coiled-coil association affinity, readily tuned by amino acid sequence, as a means to predictably alter properties of these supramolecular assemblies. A series of dimeric coiled-coil peptide sequences with identical quaternary folded structures but systematically altered folded stability were designed and biophysically characterized. The sequences were cross-linked to generate a series of branched, self-assembling biomacromolecular subunits. A clear relationship is observed between coiled-coil association affinity and apparent hydrodynamic diameter of the supramolecular polymers formed by these subunits. Our results provide a family of soluble supramolecular polymers of tunable size and well-characterized coiled-coil sequences that add to the library of building blocks available for use in the rational design of protein-based supramolecular biomaterials.
Tuning assembly size in Peptide-based supramolecular polymers by modulation of subunit association affinity.,Oshaben KM, Horne WS Biomacromolecules. 2014 Apr 14;15(4):1436-42. doi: 10.1021/bm5000423. Epub 2014, Mar 17. PMID:24598042[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Oshaben KM, Horne WS. Tuning assembly size in Peptide-based supramolecular polymers by modulation of subunit association affinity. Biomacromolecules. 2014 Apr 14;15(4):1436-42. doi: 10.1021/bm5000423. Epub 2014, Mar 17. PMID:24598042 doi:http://dx.doi.org/10.1021/bm5000423
