Comprehensive study of liposome-assisted synthesis of membrane proteins using a reconstituted cell-free translation system

Tatsuya Niwa, Yoshihiro Sasaki, Eri Uemura, Shugo Nakamura, Minato Akiyama, Mitsuru Ando, Shinichi Sawada, Sada Atu Mukai, Takuya Ueda, Hideki Taguchi*, Kazunari Akiyoshi

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)


Membrane proteins play pivotal roles in cellular processes and are key targets for drug discovery. However, the reliable synthesis and folding of membrane proteins are significant problems that need to be addressed owing to their extremely high hydrophobic properties, which promote irreversible aggregation in hydrophilic conditions. Previous reports have suggested that protein aggregation could be prevented by including exogenous liposomes in cell-free translation processes. Systematic studies that identify which membrane proteins can be rescued from irreversible aggregation during translation by liposomes would be valuable in terms of understanding the effects of liposomes and developing applications for membrane protein engineering in the context of pharmaceutical science and nanodevice development. Therefore, we performed a comprehensive study to evaluate the effects of liposomes on 85 aggregation-prone membrane proteins from Escherichia coli by using a reconstituted, chemically defined cell-free translation system. Statistical analyses revealed that the presence of liposomes increased the solubility of >90% of the studied membrane proteins, and ultimately improved the yields of the synthesized proteins. Bioinformatics analyses revealed significant correlations between the liposome effect and the physicochemical properties of the membrane proteins.

Original languageEnglish
Article number18025
JournalScientific reports
Publication statusPublished - 2015 Dec 15
Externally publishedYes

ASJC Scopus subject areas

  • General


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