New Inhibitors of Insulin-degrading Enzyme
Mentor/s
Dr. Benjamin J. Alper, Ph. D.
Participation Type
Poster
Abstract
Expressed in nearly all mammalian tissues, insulin-degrading enzyme (IDE) is a ubiquitous zinc endopeptidase which cleaves many peptides endogenous to humans and other organisms. IDE is implicated to hold vital roles in homeostasis, involved in several cellular pathways related to cellular growth, proteasome turnover, and heat-shock response. The enzyme also hydrolyzes several ligands of medical interest, such as insulin, amylin, and amyloid-beta peptide in vivo, and calcitonin, ghrelin, glucagon, and atrial natriuretic peptide in vitro. However, while much is known about the enzyme’s function, the mechanism of the IDE cleavage reaction remains poorly understood. The study of enzyme inhibition is a vital tool for understanding enzymatic mechanisms of action, and for drug design overall. Here, several new inhibitors of IDE are characterized. These inhibitors belong to a family of broad-spectrum antibiotics commonly employed in the field of medicine.
College and Major available
College of Arts and Sciences, Chemistry
Location
Digital Commons & West Campus 2nd Floor University Commons
Start Day/Time
4-28-2023 12:00 PM
End Day/Time
4-28-2023 2:00 PM
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 License.
Prize Categories
Most Scholarly Impact or Potential, Best Visuals, Best Writing
New Inhibitors of Insulin-degrading Enzyme
Digital Commons & West Campus 2nd Floor University Commons
Expressed in nearly all mammalian tissues, insulin-degrading enzyme (IDE) is a ubiquitous zinc endopeptidase which cleaves many peptides endogenous to humans and other organisms. IDE is implicated to hold vital roles in homeostasis, involved in several cellular pathways related to cellular growth, proteasome turnover, and heat-shock response. The enzyme also hydrolyzes several ligands of medical interest, such as insulin, amylin, and amyloid-beta peptide in vivo, and calcitonin, ghrelin, glucagon, and atrial natriuretic peptide in vitro. However, while much is known about the enzyme’s function, the mechanism of the IDE cleavage reaction remains poorly understood. The study of enzyme inhibition is a vital tool for understanding enzymatic mechanisms of action, and for drug design overall. Here, several new inhibitors of IDE are characterized. These inhibitors belong to a family of broad-spectrum antibiotics commonly employed in the field of medicine.
Students' Information
Jake Sarno, BS-Biochemistry/MS-Chemistry, Graduation: May 2023