Reverse Micelles

Reverse micelles (RMs) are spontaneously organizing complexes composed of surfactants with tendency toward negative curvature that surround nanoscale water pools dispersed in nonpolar solvents such as the alkanes. RMs have been used for decades in a wide array of applications from synthetic chemistry to environmental remediation to molecular biophysics. Importantly for our studies, the laboratory of A. Joshua Wand has developed and optimized methods for stable encapsulation of proteins in RMs. We take advantage of this technology to facilitate molecular biophysics studies of proteins by fluorescence spectroscopy and by NMR. In these applications, the RMs serve as nanoscale labs for investigating the influence of confinement and interfacial interactions on protein stability and dynamics, measuring the dynamics of water molecules near protein surfaces, and characterizing the structures of proteins that are normally too large for typical NMR approaches. These studies are currently supported by funds from the National Science Foundation (MCB-1942957).

In addition to their utility for studying proteins, RMs are useful as nanoreactors capable of accelerating chemical reactions and controlling synthesis of nanoparticles. These applications depend on the rate at which RMs exchange contents, and we are using stopped-flow fluorescence measurements and NMR to characterize the relationship between RM exchange and RM composition. These efforts are supported by funds from the American Chemical Society Petroleum Research Fund (PRF # 61678-UR6). What we learn from these studies informs our efforts to optimize nanoparticle synthesis using the RM method and to develop RM-based platforms for long-term storage and delivery of protein therapeutics.