ArticleLangmuir : the ACS journal of surfaces and colloids2010
Design, synthesis, and properties of branch-chained maltoside detergents for stabilization and crystallization of integral membrane proteins: human connexin 26.
Article in Langmuir : the ACS journal of surfaces and colloids, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Improved Pendant-Bearing Glucose-Neopentyl Glycols for Membrane Protein Stability.Bioconjugate chemistry · 2025Article
- Multiple Pendants-Bearing Triglucosides for Membrane Protein Studies: Effects of Pendant Length and Number on Micelle Interior Hydration and Protein Stability.Biomacromolecules · 2025Article
- Catalytically Cleavable Detergent for Membrane Protein Studies.ACS omega · 2021Article
- Cyclohexyl-α maltoside as a highly efficient tool for membrane protein studies.Current research in structural biology · 2021Article
- Pendant-bearing glucose-neopentyl glycol (P-GNG) amphiphiles for membrane protein manipulation: Importance of detergent pendant chain for protein stabilization.Acta biomaterialia · 2020Article
- Chemical tools for membrane protein structural biology.Current opinion in structural biology · 2019Review
- Conformationally Restricted Monosaccharide-Cored Glycoside Amphiphiles: The Effect of Detergent Headgroup Variation on Membrane Protein Stability.ACS chemical biology · 2019Article
- A survey of detergents for the purification of stable, active human cystic fibrosis transmembrane conductance regulator (CFTR).Biochimica et biophysica acta · 2014Article
- Steroid-based facial amphiphiles for stabilization and crystallization of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Synthesis and properties of dodecyl trehaloside detergents for membrane protein studies.Langmuir : the ACS journal of surfaces and colloids · 2012Article
- Evidence for an intermediate conformational state of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Ice breaking in GPCR structural biology.Acta pharmacologica Sinica · 2012Review
- New amphiphiles for membrane protein structural biology.Methods (San Diego, Calif.) · 2011Review
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Authors and funding
6 authors.
Funding
Abstract
A challenging requirement for structural studies of integral membrane proteins (IMPs) is the use of amphiphiles that replicate the hydrophobic environment of membranes. Progress has been impeded by the limited number of useful detergents and the need for a deeper understanding of their structure-activity relationships. To this end, we designed a family of detergents containing short, branched alkyl chains at the interface between the polar head and the apolar tail. This design mimics the second aliphatic chain of lipid molecules and reduces water penetration, thereby increasing the hydrophobicity within the interior of the micelle. To compare with the popular straight-chained maltoside detergents, the branch-chained beta-D-maltosides were synthesized efficiently in pure anomeric form. The branch-chained maltosides form smaller micelles by having shorter main chains, while having comparable hydrophobicity to the detergents with only straight chains. Selected branch-chained and straight-chained maltoside detergents were examined for their ability to solubilize, stabilize, and aid the crystallization of human connexin 26, an alpha-helical IMP that forms hexamers. We showed that the branch-chained maltosides with optimized micellar properties performed as well as or better than the straight-chained analogues and enabled crystallization in different space groups.
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