Foldable Detergents for Membrane Protein Stability

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.

Automated summary

Detergents with multiple tail and head groups have been widely used for structural studies of membrane proteins. Recent research has shown that these detergents, despite having large inter-alkyl chain distances, can effectively stabilize membrane proteins. This is achieved by incorporating a flexible spacer between two triazine rings in the detergent's linker region, allowing it to fold into a compact architecture in micellar environments. The foldability of detergents represents a new concept for detergent design and has significant potential for future development.