Institute of Organic and Pharmaceutical Chemistry
The National Hellenic Research Foundation
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Ribonucleases
RNases and in particular RNase A, have proven to be excellent model systems for the study of protein structure, folding and stability, and enzyme catalysis, resulting in four Nobel Prize lectures in chemistry (C.B. Anfinsen, W.H. Stein and S. Moore, 1972; R.B. Merrifield, 1984).
The project targets selected human ribonucleases (RNases) for the discovery of novel pharmaceutics to combat cancer and inflammatory processes. The targeted human RNases are proteins involved in angiogenesis and in the immune response system, displaying pathological side effects during cancer and inflammatory disorders. These RNases belong to the RNase A superfamily which is in fact the only enzyme family restricted to vertebrates.
The project
mainly, focuses on three human RNases:
eosinophil-derived neurotoxin (EDN; RNase 2), eosinophil
cationic protein (ECP; RNase 3) and angiogenin (Ang; RNase
5), and bovine seminal RNase (BS-RNase). We are also
using RNase A as a model system for our studies. We are using
X-ray macromolecular crystallography, and molecular
modelling to study the molecular recognition of small
molecules by target RNases with the goal to discover novel
chemical entities for the development of potent inhibitors
as potential drugs to treat the associated human diseases.
Research Interests:
Control of glycogen metabolism
Phosphoenolpyruvate carboxykinase
Carbohydrate
recognition
Human TAFs9 proteins
Xylanases and feruloyl esterases
