Glucose-oxidase based self-destructing polymeric vesicles

We have designed oxidation-responsive vesicles from synthetic amphiphilic block copolymers ("polymersomes") of ethylene glycol and propylene sulfide. Thioethers in the hydrophobic poly(propylene sulfide) block are converted into the more hydrophilic sulfoxides and sulfones upon exposure to an oxidative environment, changing the hydrophilic-lipophilic balance of the macroamphiphile and thus inducing its solubilization. Here we sought to explore generation of the oxidative environment and induction of polymersome destabilization through production of hydrogen peroxide by the glucose-oxidase (GOx)/glucose/oxygen system. We studied the encapsulation of GOx within polymersomes, its stability and activity, and glucose-triggered polymersome destabilization. Stimulus-responsive polymersomes may find applications as nanocontainers in sensing devices and as drug delivery systems.     

Breakdown kinetics of aggregates from poly(ethylene glycol‐bl‐propylene sulfide) di‐ and triblock copolymers induced by a non‐ionic surfactant

We explored the effects of addition of the nonionic surfactant Triton X‐100 on the stability of aggregates of poly(ethylene glycol‐bl‐propylene sulfide) di‐ and triblock copolymers. Fluorescence spectra of pyrene, used as a probe molecule, elucidated the various stages of transformation from pure copolymeric micelles to surfactant‐rich micelles. Turbidity measurements yielded insight into the mechanism of the interaction, the hydrophobicity of the copolymer driving the process. Triton X‐100 tends to strongly interact with highly hydrophobic copolymers by inserting into the core of the micellar aggregates. On the other hand, Triton X‐100 tends to interact with the corona of micelles formed by less hydrophobic copolymers which, for this reason, are more stable upon addition of this destabilizing agent. Kinetic data give evidence that only monomers, not micelles of surfactant, interact with the copolymer micelles. © 2008 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 46: 2477–2487, 2008     

Resolving Conformational and Rotameric Exchange in Spin-Labeled Proteins Using Saturation Recovery EPR

The function of many proteins involves equilibria between conformational substates, and to elucidate mechanisms of function it is essential to have experimental tools to detect the presence of conformational substates and to determine the time scale of exchange between them. Site-directed spin labeling (SDSL) has the potential to serve this purpose. In proteins containing a nitroxide side chain (R1), multicomponent electron paramagnetic resonance (EPR) spectra can arise either from equilibria involving different conformational substates or rotamers of R1. To employ SDSL to uniquely identify conformational equilibria, it is thus essential to distinguish between these origins of multicomponent spectra. Here we show that this is possible based on the time scale for exchange of the nitroxide between distinct environments that give rise to multicomponent EPR spectra; rotamer exchange for R1 lies in the ≈0.1–1 μs range, while conformational exchange is at least an order of magnitude slower. The time scales of exchange events are determined by saturation recovery EPR, and in favorable cases, the exchange rate constants between substates with lifetimes of approximately 1–70 μs can be estimated by the approach.     

Thick Coating and Functionalization of Organic Surfaces via ATRP in Water

Atom‐transfer radical polymerization has been used for polymerizing water‐soluble monomers from solid polymeric particles, intended as a model for any polymeric functional surface. Depending on the polarity of substrate and solvent, homogeneous initiation throughout the particles or pure surface initiation could be obtained. In the last case, polymer layers were obtained with thicknesses up to several tens of microns, still active for block copolymerization.