title: Self-sorting heterodimeric coiled coil peptides with defined and tuneable self-assembly properties.
abstract: Coiled coils with defined assembly properties and dissociation constants are highly attractive components in synthetic biology and for fabrication of peptide-based hybrid nanomaterials and nanostructures. Complex assemblies based on multiple different peptides typically require orthogonal peptides obtained by negative design. Negative design does not necessarily exclude formation of undesired species and may eventually compromise the stability of the desired coiled coils. This work describe a set of four promiscuous 28-residue de novo designed peptides that heterodimerize and fold into parallel coiled coils. The peptides are non-orthogonal and can form four different heterodimers albeit with large differences in affinities. The peptides display dissociation constants for dimerization spanning from the micromolar to the picomolar range. The significant differences in affinities for dimerization make the peptides prone to thermodynamic social self-sorting as shown by thermal unfolding and fluorescence experiments, and confirmed by simulations. The peptides self-sort with high fidelity to form the two coiled coils with the highest and lowest affinities for heterodimerization. The possibility to exploit self-sorting of mutually complementary peptides could hence be a viable approach to guide the assembly of higher order architectures and a powerful strategy for fabrication of dynamic and tuneable nanostructured materials.
authors.affiliation: Division of Molecular Physics, Department of Physics, Chemistry and Biology, Linköping University, 581 83 Linköping, Sweden.
authors.forename: Christopher
authors.initials: C
authors.lastname: Aronsson
authors.affiliation: Division of Molecular Physics, Department of Physics, Chemistry and Biology, Linköping University, 581 83 Linköping, Sweden.
authors.forename: Staffan
authors.initials: S
authors.lastname: Dånmark
authors.affiliation: School of Materials Science and Engineering, Nanyang Technological University, Singapore 639798.
authors.forename: Feng
authors.initials: F
authors.lastname: Zhou
authors.affiliation: Vehicular Systems, Department of Electrical Engineering, Linköping University, 581 83 Linköping, Sweden.
authors.forename: Per
authors.initials: P
authors.lastname: Öberg
authors.affiliation: Division of Molecular Physics, Department of Physics, Chemistry and Biology, Linköping University, 581 83 Linköping, Sweden.
authors.forename: Karin
authors.initials: K
authors.lastname: Enander
authors.affiliation: School of Materials Science and Engineering, Nanyang Technological University, Singapore 639798.
authors.forename: Haibin
authors.initials: H
authors.lastname: Su
authors.affiliation: Division of Molecular Physics, Department of Physics, Chemistry and Biology, Linköping University, 581 83 Linköping, Sweden.
authors.forename: Daniel
authors.initials: D
authors.lastname: Aili
mesh_terms: D020816:Amino Acid Motifs; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry*; D011489:Protein Denaturation; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D010455:Peptides