Enzyme-Mediated Directional Transport of a Small-Molecule Walker With Chemically Identical Feet.

ABSTRACT: We describe a small-molecule "walker" that uses enzyme catalysis to discriminate between the relative positions of its "feet" on a track and thereby move with net directionality. The bipedal walker has identical carboxylic acid feet, and "steps" along an isotactic hydroxyl-group-derivatized polyether track by the formation/breakage of ester linkages. Lipase AS catalyzes the selective hydrolysis of the rear foot of macrocyclized walkers (an information ratchet mechanism), the rear foot producing an (R)-stereocenter at its point of attachment to the track. If the hydrolyzed foot reattaches to the track in front of the bound foot it forms an (S)-stereocenter, which is resistant to enzymatic hydrolysis. Only macrocyclic walker-track conjugates are efficiently hydrolyzed by the enzyme, leading

SUBMITTER: Martin CJ 

PROVIDER: S-EPMC5618142 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature