Premium
Rationally Engineered Tandem Facial Amphiphiles for Improved Membrane Protein Stabilization Efficacy
Author(s) -
Das Manabendra,
Du Yang,
Mortensen Jonas S.,
Hariharan Parameswaran,
Lee Hyun Sung,
Byrne Bernadette,
Loland Claus J.,
Guan Lan,
Kobilka Brian K.,
Chae Pil Seok
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800388
Subject(s) - linker , membrane , chemistry , membrane protein , tandem , amide , amphiphile , biophysics , stereochemistry , combinatorial chemistry , biochemistry , materials science , organic chemistry , biology , copolymer , computer science , polymer , composite material , operating system
A new family of tandem facial glucosides/maltosides (TFGs/TFMs) for membrane protein manipulation was prepared. The best detergent varied depending on the hydrophobic thickness of the target protein, but ether‐based TFMs (TFM‐C0E, TFM‐C3E, and TFM‐C5E) were notable for their ability to confer higher membrane protein stability than the previously developed amide‐based TFA‐1 (P. S. Chae, K. Gotfryd, J. Pacyna, L. J. W. Miercke, S. G. F. Rasmussen, R. A. Robbins, R. R. Rana, C. J. Loland, B. Kobilka, R. Stroud, B. Byrne, U. Gether, S. H. Gellman, J. Am. Chem. Soc. 2010, 132, 16750–16752 ). Thus, this study not only introduces novel agents with the potential to be used in membrane protein research but also highlights the importance of both the hydrophobic length and linker functionality of the detergent in stabilizing membrane proteins.