Spatiotemporal Control Over Biosupramolecular Assembly and Catalysis

Abstract

Supramolecular self-assembly is a critical process in living organisms, precisely regulated to occur at specific newlinetimes and locations through complex reaction-diffusion mechanisms.1 This regulation is essential for various newlinecellular functions, relying on the spatiotemporal control of directed self-assembly mediated by enzymatic newlineactivity, independent of external stimuli. Despite its importance in bridging supramolecular chemistry to newlinebiomedicine, the potential of complex biosupramolecular assembly to influence spatiotemporally tunable newlineassembly formation, colloidal transport, catalysis, or phoresis has yet to be fully explored. newlineTo achieve this, first, we investigated the spatiotemporal dynamics of surfactant self-assembly driven by newlineadenosine triphosphate (ATP) and its degrading enzymes. Alkaline phosphatase (ALP) produces transient newlineassemblies, while hexokinase (HK) promotes sustained assemblies. We established concentration gradients of newlineenzymes and surfactants to program self-assembly in two-dimensional space, demonstrating a novel method newlinefor achieving spatial adaptability in self-organized systems.2 We also explored the assembly of three enzymes newlineinvolved in cascade reactions at the oil-water interface stabilized by a Zn(II)-metallosurfactant. Catalytically newlineactive clusters were formed in a binary mixture with a non-catalytic surfactant, with catalytic activity newlinemodulated by phosphate ions. This work underscores the functional diversity of supramolecular newlinenanoarchitectonics at interfaces.3 Next, we investigated the phoretic behavior of a biocolloid composed of a newlineZn(II)-coordinated metallomicelle and the enzymes horseradish peroxidase (HRP) and glucose oxidase (GOx) newlineunder microfluidic conditions. We demonstrated that an ATP-independent oxidative biocatalytic product newlineformation zone can be modulated by glucose and ATP gradients, revealing that transport direction and extent newlinecan be adjusted without ATPase involvement.4 Additionally, we developed an effective method for unactivated newlinephosphoester hydrolysis,