Development of mechanism-based inhibitors of mammalian/human DNA methyltransferases with IC50 values below 50 nM. The most successful inhibitors can be used for control of functional organization of mammalian genome in research laboratories, biotechnology, and ultimately in clinics for treatment of pathogenic mechanisms related to epigenetic processes (i.e. tissue regeneration, oncogenesis, psychiatric and neurological disorders, viral infections, immunological disorders).
Development of novel bivalent mechanism-based inhibitors of membrane-embedded protease γ-secretase. The most successful compounds can be used for treatment and early-diagnosis of Alzheimer’s disease, or for control of different physiological processes that depend on cell-to-cell communication. Paid consultant for pharmaceutical industry, γ-secretase modulators and assays.
Development and commercialization of inhibitors and modulators of human DNA methyltransferase Dnmt1 and membrane embedded protease γ-secretase.
Major Accomplishments and Perspective
Enzymatic mechanism, regulation, and novel drug-design strategies. Present research work: Development of mechanism-based inhibitors of mammalian/human DNA methyltransferases.
Membrane-embedded protease γ-secretase
Enzymatic mechanism, regulation and novel drug-design and early diagnostic strategies for Alzheimer’s disease. Present research work: Development of novel bivalent mechanism-based inhibitors of membrane-embedded protease γ-secretase.
Substrate channeling in transient protein-protein interactions. Further research work in perspective.
Mentoring individual students in research and thesis preparation.
Invited lectures: molecular mechanisms in Alzheimer’s disease or molecular mechanisms in epigenetics.
Molecular mechanisms in epigenetics and chromatin organization; molecular mechanisms in Alzheimer’s disease; protein-protein and protein-ligand interactions; assay-development and drug-design based on enzyme structure-function principles; substrate channeling.
Enzymology: in vitro, in vivo and in silico approaches for studies of structure and function of biomolecules.
Project: Enzymology of protein phosphatase CDC25B with Cdk2/CycA protein complex as the substrate (Cdk2 = cycline dependent kinase 2; CycA = cyclin A). Project Leader: Asisstant Professor Johannes Rudolph
Nikolić P., Miletić V., and Svedružić, Ž. M.DNA Methyltransferase Dnmt1: Regulation of Substrate Selectivity. In 6th OEGMBT Annual Meeting 2014 Abstract Book, edited by Alexandra Khassidov, Walter Glaser, and Christoph Klimek, 129. Vienna, Austria: Austrian Association of Molecular Life Sciences; Biotechnology; Servicebetrieb ÖH-Uni Graz GmbH. (2014).
Svedružić, Ž. M. and Reich N. O. Enzymatic properties of mouse cytosine DNA methyltransferase DNMT1. Abstracts of Papers of the American Chemical Society 223:C75. (2002).
My name is pronounced as Zhelko Svedruzhich, with "zh" pronounced as letters "asu" in words like: "treasure", "pleasure", "measure".
My name appears on papers in different forms. Some of them are Svedruzic, ZM, Svedruzic, Z. M., Svedružić, ŽM, and Svedružić, Ž. M. Name will appear with or without Croatian accents depending on the publication.