Richard Vachet
Professor
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
Arden, B. G.; Borotto, N. B.; Burant, B.; Warren, W.; Akiki, C.; Vachet, R. W. “Energy Barrier for the Amyloidogenic Structural Change of an Amyloid Forming Protein,” Anal. Chem. 2020, 92, 4731-4735.
Marcinko, T. M.; Drews, T.; Liu, T.; Vachet, R. W. “Epigallocatechin-3-gallate Inhibits Cu(II)-induced β-2-microglobulin Amyloid Formation by Binding to the Edge of its β-sheets,” Biochemistry 2020, 59, 1093-1103.
Limpikirati, P.; Pan, X.; Vachet, R. W. “Covalent Labeling with Diethylpyrocarbonate: Sensitive to Residue Microenvironment, Providing Improved Analysis of Protein Higher Order Structure by Mass Spectrometry,” Anal. Chem. 2019, 91, 8516-8523.
Liu, T.; Limpikirati, P.; Vachet, R. W. “Synergistic Structural Information from Covalent Labeling and Hydrogen-Deuterium Exchange Mass Spectrometry for Protein-Ligand Interactions” Anal. Chem. 2019, 91, 15248-15254.
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.