Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins

Pil Seok Chae, Søren G F Rasmussen, Rohini R. Rana, Kamil Gotfryd, Richa Chandra, Michael A. Goren, Andrew C. Kruse, Shailika Nurva, Claus J. Loland, Yves Pierre, David Drew, Jean Luc Popot, Daniel Picot, Brian G. Fox, Lan Guan, Ulrik Gether, Bernadette Byrne, Brian Kobilka, Samuel H. Gellman

Research output: Contribution to journalArticleResearchpeer-review

266 Citations (Scopus)


The understanding of integral membrane protein (IMP) structure and function is hampered by the difficulty of handling these proteins. Aqueous solubilization, necessary for many types of biophysical analysis, generally requires a detergent to shield the large lipophilic surfaces of native IMPs. Many proteins remain difficult to study owing to a lack of suitable detergents. We introduce a class of amphiphiles, each built around a central quaternary carbon atom derived from neopentyl glycol, with hydrophilic groups derived from maltose. Representatives of this maltose-neopentyl glycol (MNG) amphiphile family show favorable behavior relative to conventional detergents, as manifested in multiple membrane protein systems, leading to enhanced structural stability and successful crystallization. MNG amphiphiles are promising tools for membrane protein science because of the ease with which they may be prepared and the facility with which their structures may be varied.

Original languageEnglish
Pages (from-to)1003-1008
Number of pages6
JournalNature Methods
Issue number12
Publication statusPublished - Dec 2010
Externally publishedYes

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