|Title||Recombinant expression of computationally designed peptide-bundlemers in Escherichia coli.|
|Publication Type||Journal Article|
|Year of Publication||2021|
|Authors||Sinha, NJ, Kloxin, CJ, Saven, JG, Jensen, GV, Kelman, Z, Pochan, DJ|
|Date Published||2021 Mar 20|
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.
|Alternate Journal||J Biotechnol|