Journal ArticleDOI
Production of recombinant peptides as fusions with SUMO
Makkapati Satakarni,Robin Curtis +1 more
Reads0
Chats0
TLDR
This work has used SUMO protein as a fusion partner for the production of difficult-to-express, antimicrobial, self-assembling and amyloidogenic peptides using Escherichia coli to demonstrate that SUMO fusion technology is a promising alternative for production of peptides in E. coli.About:
This article is published in Protein Expression and Purification.The article was published on 2011-08-01. It has received 55 citations till now. The article focuses on the topics: Fusion protein & SUMO protein.read more
Citations
More filters
Journal ArticleDOI
Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system
TL;DR: An overview of current strategies to improve recombinant protein production in E. coli is provided, including the key factors for successful protein production, highlighting solubleprotein production, and a comprehensive summary of the latest available and traditionally used gene fusion technologies.
Journal ArticleDOI
Directed Evolution of Enzymes for Industrial Biocatalysis
TL;DR: The aim of this review is to provide an overview of current industrial applications of enzyme technology and to show how directed evolution can be used to modify and to enhance enzyme properties.
Journal ArticleDOI
Advanced technologies for improved expression of recombinant proteins in bacteria: perspectives and applications
TL;DR: An impression of expression technologies developed in recent times for enhanced production of heterologous proteins in E. coli are provided, which are of foremost importance for diverse applications in microbiology and biopharmaceutical production.
Book ChapterDOI
Tagging recombinant proteins to enhance solubility and aid purification.
Dermot Walls,Sinéad T. Loughran +1 more
TL;DR: A range of established and more recently developed solubility-enhancing and affinity tags are described, which have become indispensable tools for structural and functional proteomic initiatives that involve the expression of many proteins in parallel.
Journal ArticleDOI
Antimicrobial macromolecules: synthesis methods and future applications
TL;DR: Recent advances and challenges in the manufacture and application of antimicrobial macromolecules are summarized and their applications in addressing challenges associated with infectious disease and antibiotic-resistance are discussed.
References
More filters
Journal ArticleDOI
Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase.
D B Smith,Kevin S. Johnson +1 more
TL;DR: Plasmid expression vectors have been constructed that direct the synthesis of foreign polypeptides in Escherichia coli as fusions with the C terminus of Sj26, a 26-kDa glutathione S-transferase (GST; EC 2.5.1.18) encoded by the parasitic helminth Schistosoma japonicum.
Journal ArticleDOI
Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems.
TL;DR: An overview of the most frequently used and interesting recombinant hybrids containing a polypeptide fusion partner, termed affinity tag, to facilitate the purification of the targetpolypeptides are given.
Journal ArticleDOI
A Thioredoxin Gene Fusion Expression System That Circumvents Inclusion Body Formation in the E. coli Cytoplasm
Edward R. Lavallie,Elizabeth A. DiBlasio,Sharlotte Kovacic,Kathleen L. Grant,Paul Schendel,John M. Mccoy +5 more
TL;DR: It is found that linkage to thioredoxin dramatically increases the solubility of heterologous proteins synthesized in the E. coli cytoplasm, and that thiOREDoxin fusion proteins usually accumulate to high levels.
Journal ArticleDOI
The purification of eukaryotic polypeptides synthesized in Escherichia coli.
TL;DR: From the increasing number of reports of eukaryotic polypeptide synthesis in E. coli it is clear that the mode of expression affects not only the efficiency of production, but the nature of the polypePTide product itself.
Journal ArticleDOI
Design of nanostructured biological materials through self-assembly of peptides and proteins.
TL;DR: Several self-assembling peptide and protein systems that form nanotubes, helical ribbons and fibrous scaffolds have recently emerged as biological materials, inspiring the design of new materials for a wide range of applications in nano-biotechnology.