P1-0208 — Annual report 2012
1.
Dual inhibitor of MurD and MurE ligases from Escherichia coli and Staphylococcus aureus

MurD and MurE ligases, consecutive enzymes participating in the intracellular steps of bacterial peptidoglycan biosynthesis, are important targets for antibacterial drug discovery. We have designed, synthesized and evaluated the first D-glutamic acid-containing dual inhibitor of MurD and MurE ligases from Escherichia coli and Staphylococcus aureus (IC50s between 6.4 and 180 [micro]M possessing antibacterial activity against Gram-positive S. aureus and its methicillin-resistant strain (MRSA) with minimal inhibitory concentration (MIC) values of 8 [micro]g/mL. The inhibitor was also found to be non-cytotoxic for human HepG2 cells at concentrations below 200 [micro]M.

COBISS.SI-ID: 3274865
2.
Selective cytotoxicity of amidinopiperidine based compounds towards burkittʼs lymphoma cells involves proteasome inhibition

A set of 16 synthetized serine protease inhibitors with either N'-acyl-2-naphthohydrazide or N'-acyl-naphthalene-2-sulfonohydrazide scaffold were evaluated on different cell lines and we found that inhibitors with the N-amidinopiperidine moiety displayed selective cytotoxicity towards Burkitt's lymphoma cells (Ramos and Daudi) through the induction of caspase-dependent apoptosis.

COBISS.SI-ID: 3286129
3.
Človeške aldo-ketoreduktaze 1C1-1C4 (AKR1C1-AKR1C4) imajo vlogo 3-keto-, 17-keto- in 20-ketosteroid reduktaz, ki regulirajo aktivnost androgenov, estrogenov in progesterona. AKR1C encimi predstavljajo pomembne tarče za razvoj novih zdravilnih učinkovin. Izvedli smo virtualno rešetanje na knjižnici fragmentov in nato biokemično vrednotenje na AKR1C1-AKR1C4 encimih. Odkrili smo 24 strukturno različnih spojin z aktivnostmi v nizkem uM območju na AKR1C1, AKR1C3 ali obeh. Dva najboljša inhibitorja na AKR1C3 sta imela Ki vrednosti 0.1 in 2.7 uM in tako predstavljata odlično izhodišče za optimizacijo od zadetka do spojine vodnice.

Human aldo-keto reductases 1C1-1C4 (AKR1C1-AKR1C4) are 3-keto-, 17-keto- and 20-ketosteroid reductases that regulate the activity of androgens, estrogens and progesterone and. AKR1C enzymes represent important targets for development of new drugs. We performed a virtual high-throughput screen of a fragment library followed by biochemical evaluation on AKR1C1-AKR1C4 enzymes. We discovered 24 structurally diverse compounds with low muM Ki values for AKR1C1, AKR1C3, or both. Two of the best selective AKR1C3 inhibitors had Ki values of 0.1 muM and 2.7 muM and thus represent an excellent starting pointfor further hit-to-lead development.

COBISS.SI-ID: 30078937
4.
Immunomodulatory properties of novel nucleotide oligomerization domain 2 (Nod2) agonistic desmuramyldipeptides

The minimal bioactive structure of bacterial peptidoglycan (PGN), muramyl dipeptide (MDP) and its derivative murabutide (MB), have long been known for their adjuvant activities. For this reason, a series of novel desmuramyl dipeptides have been designed and synthesized as part of our search for therapeutically useful MDP analogues. Since nucleotide oligomerization domain 2 (Nod2) is a putative receptor for MDP, we used engineered HEK293 cells overexpressing Nod2 to screen and validate our compounds for their Nod2-agonist activity. Their immunomodulatory properties were subsequently assessed in vitro, by evaluating their effect on proinflammatory cytokine production of phorbol 12-myristate 13-acetate (PMA)/ionomycin-stimulated human peripheral blood mononuclear cells (PBMC). Herein, we present novel desmuramyl dipeptides, the most active of them possessing immunoenhancing properties as a result of their potent Nod2-agonistic effect.

COBISS.SI-ID: 3274353
5.
Novel 1,4-benzoxazine and 1,4-benzodioxine inhibitors of angiogenesis

We designed and synthesized 1,4-benzoxazine and 1,4-benzodioxine esters which combine thrombin inhibitory and GPIIb/IIIa antagonistic activity in one molecule. They were shown to inhibit endothelial cell migration and tube formation in vitro and angiogenesis in the chicken chorioallantoic membrane (CAM) assay. The corresponding carboxylic acids were devoid of antiangiogenic activity, most probably due to their insufficient entry into the cell. Although thrombin inhibition remains the most probable explanation for their inhibition of angiogenesis, VEGFR2 kinase assay suggest that other targets such as VEGFR2 might be involved.

COBISS.SI-ID: 3331441