Purification of recombinant proteins by fusion with thermally-responsive polypeptides - PubMed (original) (raw)

. 1999 Nov;17(11):1112-5.

doi: 10.1038/15100.

Affiliations

Purification of recombinant proteins by fusion with thermally-responsive polypeptides

D E Meyer et al. Nat Biotechnol. 1999 Nov.

Abstract

Elastin-like polypeptides (ELPs) undergo a reversible, inverse phase transition. Below their transition temperature (Tt), ELPs are soluble in water, but when the temperature is raised above Tt, 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.

PubMed Disclaimer

Publication types

MeSH terms

Substances

LinkOut - more resources