The Maltose-Neopentyl Glycol (MNG) amphiphiles outperform convententional detergents for stabilizing and extracting integral membrane proteins.
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.
More information on the MNG amphiphiles can be found in the January 2011 PSI SBKB technical highlight at http://sbkb.org/update/research/a-new-amphiphile-for-crystallizing-membrane-proteins.
Chemical structures of MNG amphiphiles (MNG-1, MNG-2 and MNG-3).
Chae PS, Rasmussen SG, Rana RR, Gotfryd K, Chandra R, Goren MA, Kruse AC, Nurva S, Loland CJ, Pierre Y, Drew D, Popot JL, Picot D, Fox BG, Guan L, Gether U, Byrne B, Kobilka B, Gellman SH. "Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins." Nat. Methods 7:1003-8 (2010). PubMed ID: 21037590 | Search SBKB Publications portal | PMC Link
Brian Fox, Email: firstname.lastname@example.org
Transmembrane Protein Center
Last edited:Wed 26 Sep 2012 - 6 years, 5 months ago