Research areas include microfluidics, soluble and membrane protein structure determination, protein crystallography, protein structural dynamics, biomimetic microenvironments, and tailoring protein activity and stability.
Research in the Perry Lab utilizes self-assembly, molecular design, and microfluidic technologies to generate biologically relevant microenvironments to study and enable the implementation of biomolecules to address real-world challenges. Individually, microfluidics represents an enabling technology for small volume, high-throughput analyses, while control over molecular interactions in self-assembling polyelectrolyte systems can be used to examine the interplay between biomacromolecules and the intracellular environment. Together, these capabilities can be coupled to mediate protein stability and enable both static and dynamic structural analysis of membrane proteins and other challenging targets that are not amenable to traditional analyses.
By utilizing integrated microfluidic platforms we can enable the determination of protein structural dynamics for a wide range of high-impact targets that had previously been considered inaccessible, including disease-specific proteins and medically relevant drug targets. Protein structure determination relies on the growth of high quality protein crystals for X-ray diffraction analysis. However, identification of suitable conditions for protein crystallization requires extensive testing, and any resulting crystals tend to be both extremely small (micron-scale or smaller) and fragile. X-ray compatible microfluidic platforms overcome many of these challenges by enabling the high-throughput formulation of a large number of experiments while using miniscule sample volumes and facilitating analysis of crystals without harvesting them from the device. Furthermore, integrated fluid control can facilitate the controlled addition of ligands or other chemical additives for use in more complex experiments designed to capture protein structural dynamics in real-time.
The use of proteins in real-world applications such as vaccines, biocatalysis, and biosensors also requires an understanding of how proteins interact with their environment. For instance, proteins within cells are functional at very high temperatures, while purified proteins typically require refrigeration in order to remain stable. We seek to use self-assembling biomimetic polymers to understand protein-protein interactions and recapitulate the stabilizing conditions found inside of living cells. This research will benefit from the use of high-throughput microfluidic assays and from the predictive power of molecular simulations and theoretical models. Our goal is to enhance the efficacy of proteins and enzymes for a variety of applications, including protein purification, protein-based therapeutics, and models for protein aggregation diseases such as Alzheimer’s.
Learn more at www.umass.edu/perry/
- BS University of Arizona, Chemical Engineering, 2002
- BS University of Arizona, Chemistry, 2003
- MS University of Arizona, Chemical Engineering, 2005
- PhD University of Illinois at Urbana-Champaign, Chemical & Biomolecular Engineering, 2010
- Post-Doctoral Training University of California at Berkeley, Bioengineering
- Post-Doctoral Training University of Chicago, Institute for Molecular Engineering