An Engineered Lithocholate-Based Facial Amphiphile Stabilizes Membrane Proteins: Assessing the Impact of Detergent Customizability on Protein Stability
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An Engineered Lithocholate-Based Facial Amphiphile Stabilizes Membrane Proteins : Assessing the Impact of Detergent Customizability on Protein Stability. / Das, Manabendra; Du, Yang; Mortensen, Jonas S.; Bae, Hyoung Eun; Byrne, Bernadette; Loland, Claus J.; Kobilka, Brian K.; Chae, Pil Seok.
In: Chemistry - A European Journal, Vol. 24, No. 39, 11.07.2018, p. 9860-9868.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - An Engineered Lithocholate-Based Facial Amphiphile Stabilizes Membrane Proteins
T2 - Assessing the Impact of Detergent Customizability on Protein Stability
AU - Das, Manabendra
AU - Du, Yang
AU - Mortensen, Jonas S.
AU - Bae, Hyoung Eun
AU - Byrne, Bernadette
AU - Loland, Claus J.
AU - Kobilka, Brian K.
AU - Chae, Pil Seok
PY - 2018/7/11
Y1 - 2018/7/11
N2 - Amphiphiles are critical tools for the structural and functional study of membrane proteins. Membrane proteins encapsulated by conventional head-to-tail detergents tend to undergo structural degradation, necessitating the development of structurally novel agents with improved efficacy. In recent years, facial amphiphiles have yielded encouraging results in terms of membrane protein stability. Herein, we report a new facial detergent (i.e., LFA-C4) that confers greater stability to tested membrane proteins than the bola form analogue. Owing to the increased facial property and the adaptability of the detergent micelles in complex with different membrane proteins, LFA-C4 yields increased stability compared to n-dodecyl-β-d-maltoside (DDM). Thus, this study not only describes a novel maltoside detergent with enhanced protein-stabilizing properties, but also shows that the customizable nature of a detergent plays an important role in the stabilization of membrane proteins. Owing to both synthetic convenience and enhanced stabilization efficacy for a range of membrane proteins, the new agent has major potential in membrane protein research.
AB - Amphiphiles are critical tools for the structural and functional study of membrane proteins. Membrane proteins encapsulated by conventional head-to-tail detergents tend to undergo structural degradation, necessitating the development of structurally novel agents with improved efficacy. In recent years, facial amphiphiles have yielded encouraging results in terms of membrane protein stability. Herein, we report a new facial detergent (i.e., LFA-C4) that confers greater stability to tested membrane proteins than the bola form analogue. Owing to the increased facial property and the adaptability of the detergent micelles in complex with different membrane proteins, LFA-C4 yields increased stability compared to n-dodecyl-β-d-maltoside (DDM). Thus, this study not only describes a novel maltoside detergent with enhanced protein-stabilizing properties, but also shows that the customizable nature of a detergent plays an important role in the stabilization of membrane proteins. Owing to both synthetic convenience and enhanced stabilization efficacy for a range of membrane proteins, the new agent has major potential in membrane protein research.
KW - amphiphiles
KW - membrane proteins
KW - micelles
KW - protein stabilization
KW - protein structures
KW - Membrane Proteins/chemistry
KW - Micelles
KW - Hydrophobic and Hydrophilic Interactions
KW - Protein Stability
KW - Lithocholic Acid
KW - Detergents/chemistry
U2 - 10.1002/chem.201801141
DO - 10.1002/chem.201801141
M3 - Journal article
C2 - 29741269
AN - SCOPUS:85049774129
VL - 24
SP - 9860
EP - 9868
JO - Chemistry: A European Journal
JF - Chemistry: A European Journal
SN - 0947-6539
IS - 39
ER -
ID: 209803221