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 Juul Løland; Yves Pierre; David Drew; Jean-Luc Popot; Daniel Picot; Brian G Fox; Lan Guan; Ulrik Gether; Bernadette Byrne; Brian Kobilka; Samuel H Gellman

doi:10.1038/nmeth.1526

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 Juul Løland, Yves Pierre, David Drew, Jean-Luc Popot, Daniel Picot, Brian G Fox, Lan Guan, Ulrik Gether, Bernadette Byrne, Brian Kobilka, Samuel H Gellman

280 Citations (Scopus)

Abstract

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 language	English
Journal	Nature Methods
Volume	7
Pages (from-to)	1003-8
Number of pages	6
ISSN	1548-7091
DOIs	https://doi.org/10.1038/nmeth.1526
Publication status	Published - Dec 2010

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Chae, P. S., Rasmussen, S. G. F., Rana, R. R., Gotfryd, K., Chandra, R., Goren, M. A., Kruse, A. C., Nurva, S., Løland, C. J., Pierre, Y., Drew, D., Popot, J-L., Picot, D., Fox, B. G., Guan, L., Gether, U., Byrne, B., Kobilka, B., & Gellman, S. H. (2010). Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins. Nature Methods, 7, 1003-8. https://doi.org/10.1038/nmeth.1526

Chae, PS, Rasmussen, SGF, Rana, RR, Gotfryd, K, Chandra, R, Goren, MA, Kruse, AC, Nurva, S, Løland, CJ, Pierre, Y, Drew, D, Popot, J-L, Picot, D, Fox, BG, Guan, L, Gether, U, Byrne, B, Kobilka, B & Gellman, SH 2010, 'Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins', Nature Methods, vol. 7, pp. 1003-8. https://doi.org/10.1038/nmeth.1526

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

abstract = "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.",

author = "Chae, {Pil Seok} and Rasmussen, {S{\o}ren G F} and Rana, {Rohini R} and Kamil Gotfryd and Richa Chandra and Goren, {Michael A} and Kruse, {Andrew C} and Shailika Nurva and L{\o}land, {Claus Juul} and Yves Pierre and David Drew and Jean-Luc Popot and Daniel Picot and Fox, {Brian G} and Lan Guan and Ulrik Gether and Bernadette Byrne and Brian Kobilka and Gellman, {Samuel H}",

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T1 - Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins

AU - Chae, Pil Seok

AU - Rasmussen, Søren G F

AU - Rana, Rohini R

AU - Gotfryd, Kamil

AU - Chandra, Richa

AU - Goren, Michael A

AU - Kruse, Andrew C

AU - Nurva, Shailika

AU - Løland, Claus Juul

AU - Pierre, Yves

AU - Drew, David

AU - Popot, Jean-Luc

AU - Picot, Daniel

AU - Fox, Brian G

AU - Guan, Lan

AU - Gether, Ulrik

AU - Byrne, Bernadette

AU - Kobilka, Brian

AU - Gellman, Samuel H

PY - 2010/12

Y1 - 2010/12

N2 - 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.

AB - 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.

U2 - 10.1038/nmeth.1526

DO - 10.1038/nmeth.1526

M3 - Journal article

C2 - 21037590

SN - 1548-7091

VL - 7

SP - 1003

EP - 1008

JO - Nature Methods

JF - Nature Methods

ER -

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

Abstract

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