Designing fluorinated, sugar-based, cholesterol-derived or topologically engineered amphiphiles to tackle the toughest membrane protein challenges.
The laboratory has become a recognized expert in the rational design of innovative detergents with tunable HLB, polar headgroup topology, fluorination patterns, linker engineering and controlled rigidity. These finely tuned amphiphiles show how subtle structural modifications influence key physicochemical properties and, in turn, govern extraction efficiency, protein stability, and the size and homogeneity of protein–detergent complexes (PDCs).
By establishing systematic structure–property relationships, our team develops high-performance detergents that outperform conventional surfactants and significantly expand the molecular toolbox available for membrane protein structural biology.
Associated publications
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