Membrane proteins are amphipathic bio-macromolecules incompatible with the polar environments of
aqueous media. Conventional detergents encapsulate the hydrophobic surfaces of membrane proteins
allowing them to exist in aqueous solution. Membrane proteins stabilized by detergent micelles are used
for structural and functional analysis. Despite the availability of a large number of detergents, only a few
agents are sufficiently effective at maintaining the integrity of membrane proteins to allow successful
crystallization. In the present study, we describe a novel class of synthetic amphiphiles with a branched
tail group and a triglucoside head group. These head and tail groups were connected via an amide or
ether linkage by using a tris(hydroxylmethyl)aminomethane (TRIS) or neopentyl glycol (NPG) linker to
produce TRIS-derived triglucosides (TDTs) and NPG-derived triglucosides (NDTs), respectively. Members
of this class conferred enhanced stability on target membrane proteins compared to conventional
detergents. Because of straightforward synthesis of the novel agents and their favourable effects on
a range of membrane proteins, these agents should be of wide applicability to membrane protein science.