Recombinant expression of computationally designed peptide-bundlemers in Escherichia coli

Exact display of side chains using computational design of expressed bundlemer-forming peptides. [Display omitted] •Computationally designed coiled coil bundlemers are protein-mimicking modular building blocks for targeted self-assembly.•Recombinant expression of designed peptides in Escherichia Coli enables production of large quantities of bundlemers.•Resulting bundlemers can be used to self-assemble biomaterials for both biological and non-biological applications. Computational design of fully artificial peptides is extensively researched by material scientists and engineers for the construction of novel nanostructures and biomaterials. Such design has yielded a peptide-based building block or bundlemer, a coiled coil peptide assembly that undergoes further physical-covalent interactions to form 1D, 2D and, potentially, 3D hierarchical assemblies and displays targeted and biomimetic material properties. Recombinant expression is a convenient, flexible tool to synthesize such artificial and modified peptides in large quantities while also enabling economical synthesis of isotopically labeled peptides and longer protein-like artificial peptides. This report describes the protocol for recombinant expression of a 31-amino acid, computationally designed bundlemer-forming peptide in Escherichia coli. Peptide yields of 10 mgs per liter of media were achieved which highlights complementary advantages of recombinant expression technique relative to conventional laboratory-scale synthesis, such as solid-phase peptide synthesis.