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

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.

journal_name

Nat Biotechnol

journal_title

Nature biotechnology

authors

Meyer DE,Chilkoti A

doi

10.1038/15100

subject

Has Abstract

pub_date

1999-11-01 00:00:00

pages

1112-5

issue

11

eissn

1087-0156

issn

1546-1696

journal_volume

17

pub_type

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