Richard Vachet
Professor and Department Head
Proteins are essential players in most biological processes and unraveling their behavior (or misbehavior) is important for understanding the molecular basis of life and of a variety of diseases. My research group is interested in protein chemistry with a particular focus on the development of new methods to gather insight into protein misfolding, aggregation, protein amyloid formation, protein interactions with metals, and protein chemistry within a cell.
Current Research
We have two primary areas of investigation: (1) mass spectrometry-based methods to study protein amyloid formation and (2) elucidating the structure of the pre-amyloid oligomers of β-2-microglobulin.
Learn more at www.chem.umass.edu/~vachet/
Academic Background
- BS College of William and Mary
- PhD University of North Carolina, Chapel Hill
- NRC postdoctoral fellowship: Naval Research Laboratory
Limpikirati, P.; Liu, T.; Vachet, R. W. “Covalent Labeling-Mass Spectrometry for Studying Protein Structure and Interactions” Methods, 2018, 144, 79-93.
Liu, T.; Marcinko, T. M.; Kiefer, P. A.; Vachet, R. W. “Using Covalent Labeling and Mass Spectrometry to Study Protein Binding Sites of Amyloid Inhibiting Molecules” Anal. Chem. 2017, 89, 11583-11591.
Marcinko, T. M.; Dong, J.; LeBlanc, R.; Daborowski, K. V.; Vachet, R. W. “Small Molecule-mediated Inhibition of β-2-Microglobulin Amyloid Fibril Formation,” J. Biol. Chem. 2017, 292, 10630-10638.
Borotto, N. B.; Zhang, Z.; Dong, J.; Burant, B.; Vachet, R. W. “Increased β-Sheet Dynamics and D-E Loop Repositioning are Necessary for Cu(II)-Induced Amyloid Formation by β-2-Microglobulin” Biochemistry 2017, 56, 1095-1104.
Zhang, Z.; Vachet, R. W. “Kinetics of Protein Oligomerization Studied by Hydrogen/Deuterium Exchange and Mass Spectrometry” Anal. Chem. 2015, 87, 11777-11783.
Dong, J.; Joseph, C. A.; Borotto, N. B.; Gill, V. L.; Maroney, M. J.; Vachet, R. W. “The Unique Effect of Cu(II) in the Metal-Induced Amyloid Formation of β-2-Microglobulin” Biochemistry 2014, 53, 1263-1274.
