Recombinant expression of computationally designed peptide-bundlemers in Escherichia coli

J Biotechnol. 2021 Mar 20;330:57-60. doi: 10.1016/j.jbiotec.2021.03.004. Epub 2021 Mar 6.


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.

Keywords: Bundlemer; Computational design; Escherichia coli; Peptide; Recombinant expression; Self-assembly.

MeSH terms

  • Biocompatible Materials
  • Escherichia coli* / genetics
  • Nanostructures*
  • Peptides / genetics
  • Proteins


  • Biocompatible Materials
  • Peptides
  • Proteins