Abstract
Dipeptidyl peptidase III (DPP3) is a ubiquitously expressed zinc-dependent peptide cutting enzyme and selectively hydrolyses amide bonds to cleave N-terminal dipeptide fragments off of physiologically important oligopeptides. DPP3 has been found in a multitude of different types of cells and appears to be involved in various physiological processes (e.g. nociception, blood pressure control, protein turnover). Using the slowly converted peptide substrate tynorphin (VVYPW) as starting point, we have replaced the scissile bond with a fluoroethylene bioisostere to design ground state inhibitors, which led to the so far most effective peptide-based inhibitor of DPP3.
Originalsprache | englisch |
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Aufsatznummer | 116831 |
Fachzeitschrift | Bioorganic and Medicinal Chemistry |
Jahrgang | 67 |
DOIs | |
Publikationsstatus | Veröffentlicht - 1 Aug. 2022 |
ASJC Scopus subject areas
- Biochemie
- Molekularmedizin
- Molekularbiologie
- Pharmazeutische Wissenschaften
- Wirkstoffforschung
- Klinische Biochemie
- Organische Chemie
Fields of Expertise
- Human- & Biotechnology
Kooperationen
- BioTechMed-Graz