Marcey Waters
Glen H. Elder, Jr. Distinguished Professor
University of North Carolina
Talk Information
Implications and Applications of PTMs
19 June 2025, 01:45pm - 02:10pm, in the Pacific Jewel Ballroom
L64 – Addressing the Challenge of Selective Inhibition of Histone Trimethyllysine Reader Proteins through Electrostatic Pocket Mapping

Professor Marcey L. Waters holds the Glen H. Elder Jr. Distinguished Professorship in the Department of Chemistry at the University of North Carolina at Chapel Hill. Her research lies at the intersection of organic chemistry, chemical biology, and supramolecular chemistry, with a focus on molecular recognition and the design of synthetic receptors for biomolecular targets.
Academic Background
Dr. Waters earned her B.A. in Chemistry from the University of California, San Diego in 1992, where she conducted undergraduate research on aromaticity. She completed her Ph.D. at the University of Chicago in 1997 under the mentorship of Professor William D. Wulff, focusing on the mechanisms of carbene complex reactions. Following her doctorate, she was an NIH postdoctoral fellow in Professor Ronald Breslow’s laboratory at Columbia University, where she investigated dinuclear metalloenzyme mimics and antiaromaticity. In 1999, Dr. Waters joined the faculty at UNC-Chapel Hill, where she has since established a prominent research program.
Research Focus
Professor Waters' laboratory explores the principles of molecular recognition, particularly the role of non-covalent interactions such as π–π and cation–π interactions in peptide and protein systems. Her team designs synthetic receptors and studies their interactions with post-translational modifications like methylated lysine and arginine residues, contributing to the understanding of epigenetic regulation. Additionally, her research encompasses the development of peptidomimetics and the application of supramolecular chemistry to biological systems.
Notable Contributions
Dr. Waters has significantly advanced the field of chemical biology through her work on the design of synthetic receptors that mimic natural protein interactions. Her studies on the thermodynamics of aromatic interactions in peptides have provided insights into protein folding and stability. She has received numerous accolades, including the NSF CAREER Award, Alfred P. Sloan Fellowship, and election as a Fellow of the American Association for the Advancement of Science. From 2017 to 2019, she served as President of the American Peptide Society, reflecting her leadership in the scientific community.
Professional Engagements
Beyond her research, Professor Waters is dedicated to education and mentorship. She has been recognized with teaching awards such as the Tanner Award for Excellence in Undergraduate Teaching and the UNC University Award for the Advancement of Women. She actively participates in initiatives promoting diversity and inclusion in science and has served on editorial boards for leading journals in chemistry. Her commitment to fostering the next generation of scientists is evident through her involvement in various mentorship programs and academic leadership roles.
Through her interdisciplinary research and dedication to teaching and mentorship, Professor Marcey L. Waters continues to make impactful contributions to the fields of chemistry and chemical biology.
Addressing the Challenge of Selective Inhibition of Histone Trimethyllysine Reader Proteins through Electrostatic Pocket Mapping
UNC Chapel Hill, Dept of Chemistry
Post-translational modifications (PTMs) in histone proteins, including lysine methylation and acylation, regulate gene expression through recruitment of reader proteins to the nucleosome. Dysregulation of these events is prevalent in a wide range of diseases, such that there is much interest in developing inhibitors for these protein-protein interactions. Nonetheless, each PTM typically has numerous reader proteins that bind it, making selective inhibition a challenge. To address this challenge, we have undertaken a campaign to map the diQerences in selectivity among reader proteins via pocket mapping, using a range of histone peptides containing a range of abiotic amino acid isosteres in place of the PTMs of interest. Results of these pocket mapping eQorts will be presented.