ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022
Foldable Detergents for Membrane Protein Study: Importance of Detergent Core Flexibility in Protein Stabilization.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Recent Advances in Detergent Chemistry and Handling Support Membrane Protein Analysis Including Lipid Interactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Review
- Improved Pendant-Bearing Glucose-Neopentyl Glycols for Membrane Protein Stability.Bioconjugate chemistry · 2025Article
- Rational Approach to Improve Detergent Efficacy for Membrane Protein Stabilization.Bioconjugate chemistry · 2024Article
- Melamine-cored glucosides for membrane protein solubilization and stabilization: importance of water-mediated intermolecular hydrogen bonding in detergent performance.Chemical science · 2023Article
- CHARMM-GUIJournal of chemical theory and computation · 2023Review
- Combinatorial synthesis enables scalable designer detergents for membrane protein studies.Chemical science · 2022Article
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Authors and funding
15 authors at 8 institutions in 5 countries.
Funding
Abstract
Membrane proteins are of biological and pharmaceutical significance. However, their structural study is extremely challenging mainly due to the fact that only a small number of chemical tools are suitable for stabilizing membrane proteins in solution. Detergents are widely used in membrane protein study, but conventional detergents are generally poor at stabilizing challenging membrane proteins such as G protein-coupled receptors and protein complexes. In the current study, we prepared tandem triazine-based maltosides (TZMs) with two amphiphilic triazine units connected by different diamine linkers, hydrazine (TZM-Hs) and 1,2-ethylenediamine (TZM-Es). These TZMs were consistently superior to a gold standard detergent (DDM) in terms of stabilizing a few membrane proteins. In addition, the TZM-Es containing a long linker showed more general protein stabilization efficacy with multiple membrane proteins than the TZM-Hs containing a short linker. This result indicates that introduction of the flexible1,2-ethylenediamine linker between two rigid triazine rings enables the TZM-Es to fold into favourable conformations in order to promote membrane protein stability. The novel concept of detergent foldability introduced in the current study has potential in rational detergent design and membrane protein applications.
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Registered trials
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