Recombinant expression of computationally designed peptide-bundlemers in Escherichia coli.

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TitleRecombinant expression of computationally designed peptide-bundlemers in Escherichia coli.
Publication TypeJournal Article
Year of Publication2021
AuthorsSinha, NJ, Kloxin, CJ, Saven, JG, Jensen, GV, Kelman, Z, Pochan, DJ
JournalJ Biotechnol
Volume330
Pagination57-60
Date Published2021 Mar 20
ISSN1873-4863
Abstract

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.

DOI10.1016/j.jbiotec.2021.03.004
Alternate JournalJ Biotechnol
PubMed ID33689866