Foldable Detergents for Membrane Protein Stability
- Authors
- Youn, Taeyeol; Yoon, Soyoung; Byrne, Bernadette; Chae, Pil Seok
- Issue Date
- Oct-2022
- Publisher
- John Wiley & Sons Ltd.
- Keywords
- amphiphiles; foldable detergents; membrane proteins; protein stabilization; self-assembly
- Citation
- ChemBioChem, v.23, no.19, pp 1 - 5
- Pages
- 5
- Indexed
- SCIE
SCOPUS
- Journal Title
- ChemBioChem
- Volume
- 23
- Number
- 19
- Start Page
- 1
- End Page
- 5
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/111366
- DOI
- 10.1002/cbic.202200276
- ISSN
- 1439-4227
1439-7633
- Abstract
- Detergents are widely used for membrane protein structural study. Many recently developed detergents contain multiple tail and head groups, which are typically connected via a small and branched linker. Due to their inherent compact structures, with small inter-alkyl chain distances, these detergents form micelles with high alkyl chain density in the interiors, a feature favorably associated with membrane-protein stability. A recent study on tandem triazine maltosides (TZMs) revealed a distinct trend; despite possession of an apparently large inter-alkyl chain distance, the TZM-Es were highly effective at stabilizing membrane proteins. Thanks to the incorporation of a flexible spacer between the two triazine rings in the linker region, these detergents are prone to folding into a compact architecture in micellar environments instead of adopting an extended conformation. Detergent foldability represents a new concept of novel detergent design with significant potential for future detergent development.
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