Biochemical and Structural studies of protein targets which play important role in diseases such as diabetes mellitus type II or malaria for the purposes of structural-based drug design. My recent research interests include the cloning, expression, purification and crystallization of odorant binding proteins of mosquito Anopheles gambiae, which is responsible for the transmission of malaria, in order to design strong repellents or attractants which will impede the detection of human objective.
Watson, K.A., Chrysina, E.D., Tsitsanou K.E., Zographos, S.E., Gregoriou, M., Archontis, G., Leonidas, D.D., Oikonomakos, N.G., Johnson, L.N. and Fleet, G.W.J. (2005). Kinetic and structural studies of glucopyranose spirohydantoin and glucopyranosylamine analogues inhibitors of glycogen phosphorylase. Proteins61, 966-983.
Tsitsanou, K.E., Skamnaki, V.T. & Oikonomakos, N.G. (2000). Structural basis of the synergistic inhibition of glycogen phosphorylase a by caffeine and a potential antidiabetic drug. Árchives of Biochemistry and Biophysics348, 245-254.
Oikonomakos, N.G., Zographos, S.E., Skamnaki, V.T., Tsitsanou, K.E. & Johnson, L.N. (2000). Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site. J. Biol. Chem. 275, 34566-73.
Oikonomakos, N.G., Skamnaki, V.T., Tsitsanou, K.E., Gavalas, N.G. & Johnson, L.N. (2000). A new allosteric site in glycogen phosphorylase b as a target for drug interactions. Structure8, 575-584.
Tsitsanou, K.E., Zographos, S.E., Skamnaki, V.T. & Oikonomakos, N.G. (1999). Molecular recognition in glycogen phosphorylase inhibitor design (review). Review of Clinical Pharmacology and Pharmakokinetics13, 9-25.
Tsitsanou, K.E., Oikonomakos, N.G., Zographos, S.E., Skamnaki, V.T., Gregoriou, M., Watson, K.A., Johnson, L.N. & Fleet, G.W.J. (1999). The effect of most commonly used cryoprotectants on glycogen phosphorylase activity and structure. Protein Science 8, 741-749.
Oikonomakos, N.G., Tsitsanou, K.E., Zographos, S.E., Skamnaki, V.T., Goldmann, S. & Bischoff, H. (1999). Allosteric inhibition of glycogen phosphorylase a by the potential antidiabetic drug 3-isopropyl 4-(2-chlorophenyl)-1,4-dihydro-1-ethyl-2-methyl-pyridine-3,5,6-tricarboxylate. Protein Science8, 1930-1945.