Making water-soluble integral membrane proteins in vivo using an amphipathic protein fusion strategy

Dario Mizrachi, Yujie Chen, Jiayan Liu, Hwei-Ming Peng, Ailong Ke, Lois Pollack, Raymond J. Turner, Richard J. Auchus and Matthew P. DeLisa ()
Additional contact information
Dario Mizrachi: School of Chemical and Biomolecular Engineering, Cornell University
Yujie Chen: School of Applied and Engineering Physics, Cornell University
Jiayan Liu: University of Michigan
Hwei-Ming Peng: University of Michigan
Ailong Ke: Cornell University
Lois Pollack: School of Applied and Engineering Physics, Cornell University
Raymond J. Turner: University of Calgary
Richard J. Auchus: University of Michigan
Matthew P. DeLisa: School of Chemical and Biomolecular Engineering, Cornell University

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: Abstract Integral membrane proteins (IMPs) play crucial roles in all cells and represent attractive pharmacological targets. However, functional and structural studies of IMPs are hindered by their hydrophobic nature and the fact that they are generally unstable following extraction from their native membrane environment using detergents. Here we devise a general strategy for in vivo solubilization of IMPs in structurally relevant conformations without the need for detergents or mutations to the IMP itself, as an alternative to extraction and in vitro solubilization. This technique, called SIMPLEx (solubilization of IMPs with high levels of expression), allows the direct expression of soluble products in living cells by simply fusing an IMP target with truncated apolipoprotein A-I, which serves as an amphipathic proteic ‘shield’ that sequesters the IMP from water and promotes its solubilization.

Date: 2015
References: Add references at CitEc
Citations: View citations in EconPapers (4)

Downloads: (external link)
https://www.nature.com/articles/ncomms7826 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7826

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms7826

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().