Purification of recombinant proteins by fusion with thermally-responsive polypeptides

Elastin-like polypeptides (ELPs) undergo a reversible, inverse phase transition. Below their transition temperature (T t ), ELPs are soluble in water, but when the temperature is raised above T t , phase transition occurs, leading to aggregation of the polypeptide. We demonstrate a method for purifi...

Full description

Saved in:
Bibliographic Details
Published in:Nature biotechnology 1999-11, Vol.17 (11), p.1112-1115
Main Authors: Meyer, Dan E., Chilkoti, Ashutosh
Format: Article
Language:English
Subjects:
Agriculture
Amino Acid Sequence
Base Sequence
Bioinformatics
Biological and medical sciences
Biomedical and Life Sciences
Biomedical Engineering/Biotechnology
Biomedicine
Biotechnology
Elastin - genetics
Elastin - metabolism
Fundamental and applied biological sciences. Psychology
Life Sciences
Methods. Procedures. Technologies
Molecular Sequence Data
Others
Peptides - genetics
Peptides - metabolism
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
research-article
Thioredoxins - genetics
Thioredoxins - metabolism
Various methods and equipments
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Elastin-like polypeptides (ELPs) undergo a reversible, inverse phase transition. Below their transition temperature (T t ), ELPs are soluble in water, but when the temperature is raised above T t , phase transition occurs, leading to aggregation of the polypeptide. We demonstrate a method for purification of soluble fusion proteins incorporating an ELP tag. Advantages of this method, termed "inverse transition cycling," include technical simplicity, low cost, ease of scale-up, and capacity for multiplexing. More broadly, the ability to environmentally modulate the physicochemical properties of recombinant proteins by fusion with ELPs will allow diverse applications in bioseparation, immunoassays, biocatalysis, and drug delivery.
ISSN:1087-0156
1546-1696
DOI:10.1038/15100