ATP-fuelled self-assembly to regulate chemical reactivity in the time domain.

ABSTRACT: Here, we exploit a small biomolecule - ATP - to gain temporal control over chemical reactivity in a synthetic system composed of small self-assembling molecules and reactants. The approach relies on the capacity of ATP to template the formation of amphiphile-based assemblies. The presence of the enzyme alkaline phosphatase causes a gradual decrease in the ATP-concentration in time and, consequently, a spontaneous dissociation of the assemblies. The uptake of apolar reactants in the hydrophobic domain of the assemblies leads to an enhancement of the reaction rate. It is shown that ATP-triggered self-assembly causes the selective upregulation of one out of two hydrazone-bond formation reactions that take place concurrently in the system. This leads to an inversion in the product ratio, which

SUBMITTER: Cardona MA 

PROVIDER: S-EPMC8148039 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature