Purification of recombinant proteins by fusion with thermally-responsive polypeptides.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Meyer, DE; Chilkoti, A

Published Date

  • November 1999

Published In

Volume / Issue

  • 17 / 11

Start / End Page

  • 1112 - 1115

PubMed ID

  • 10545920

Pubmed Central ID

  • 10545920

International Standard Serial Number (ISSN)

  • 1087-0156

Digital Object Identifier (DOI)

  • 10.1038/15100

Language

  • eng

Conference Location

  • United States