Recombinant production of medium- to large-sized peptides in Escherichia coli using a cleavable self-aggregating tag.

ABSTRACT:

Background

Peptides have recently become attractive for therapeutic applications. However, efficient production of medium- to large-sized peptides (30-100 amino acids [aa]) remains challenging both by recombinant and chemical synthesis. We previously reported the formation of active enzyme aggregates in Escherichia coli cells induced by the short β-structured peptide ELK16 (LELELKLKLELELKLK) and developed a streamlined protein expression and purification approach. In this approach, a cleavable self-aggregating tag (cSAT) consisting of an intein molecule and ELK16 was used to release the recombinant peptides with reasonable purity from active aggregates.

Results

In this work, we extended the cSAT approach to a generalized expression and purification solution for a set of medi

SUBMITTER: Zhao Q 

PROVIDER: S-EPMC4975908 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature