Petra Stefanic Anderluh

University of Ljubljana, Lubliano, Ljubljana, Slovenia

Are you Petra Stefanic Anderluh?

Claim your profile

Publications (10)27.69 Total impact

  • Nenad Maras, Petra Stefanic Anderluh, Uros Urleb, Marijan Kocevar
    [Show abstract] [Hide abstract]
    ABSTRACT: ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
    ChemInform 01/2009; 40(26).
  • [Show abstract] [Hide abstract]
    ABSTRACT: Molecules regulating cell death constitute prominent therapeutic targets. The pro-apoptotic role of serine protease inhibitors prompted us to search for novel modulators of this process. We have tested some recently synthesized antithrombotic compounds for their potential to induce apoptotic cell death. Cell based analyses revealed that inhibitors built on the azaphenylalanine scaffold are, for B-cell lymphoma cells, severely cytotoxic, while other compounds tested were moderate or non-cytotoxic. These inhibitors induced the time and concentration dependent biochemical and morphological characteristics of apoptosis, such as DEVDase activation, loss of mitochondrial membrane potential, nuclear degradation and genomic DNA fragmentation. Most of the inhibitors proved to be selective for thrombin, with inhibition constants (K(i)) in the nanomolar range. However, they could also inhibit at least one additional serine protease (trypsin, chymotrypsin and/or coagulation factor X) with K(i) values in the nanomolar or low micromolar range. These serine protease inhibitors constitute novel apoptosis inducing compounds in B-cell lymphoma cells.
    European journal of pharmacology 12/2008; 602(1):15-22. · 2.59 Impact Factor
  • J Humljan, S Starcević, V Car, P Stefanic Anderluh, D Kocjan, B Jenko, U Urleb
    [Show abstract] [Hide abstract]
    ABSTRACT: UDP-N-acetylmuramic acid (UDP-MurNAc) is a substrate of MurC, an important enzyme in the intracellular pathway of bacterial peptidoglycan biosynthesis. Various approaches towards preparation of UDP-MurNAc have been published but these synthetic preparations were shown to include many problematic steps. An optimization study with the focus on muramyl phosphate and UMP-morpholidate coupling was performed, resulting in a synthetic procedure enabling robust and easily reproducible production on a multi-gram scale.
    Pharmazie 03/2008; 63(2):102-6. · 0.96 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Two new imidazo[1,2-a]pyridines, 8-hydroxyimidazo[1,2-a]pyridine-2-carboxylic acid (4) and Et 8-hydroxyimidazo[1,2-a]pyridine-2-carboxylate (6) were prepd. via cyclization of 2-aminopyridin-3-ol (1) with bromopyruvic acid (2) and Et bromopyruvate (3), resp. 8-Hydroxyimidazo[1,2-a]pyridine-2-carboxylic acid (4) was successfully coupled with various amino acid derivs. via its active ester intermediate into the corresponding amides 22-27. O-protected Et 8-hydroxyimidazo[1,2-a]pyridine-2-carboxylate 11 was transformed into its hydrazide 13, acyl azide 14, and amide 15 derivs. [on SciFinder (R)]
    Heterocycles 01/2008; 75(6):1355-1370. · 1.08 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
    ChemInform 01/2008; 39(41).
  • [Show abstract] [Hide abstract]
    ABSTRACT: A wide variety of pathogens have acquired antimicrobial resistance as an inevitable evolutionary response to the extensive use of antibacterial agents. In particular, one of the most widely used antibiotic structural classes is the beta-lactams, in which the most common and the most efficient mechanism of bacterial resistance is the synthesis of beta-lactamases. Class C beta-lactamase enzymes are primarily cephalosporinases, mostly chromosomally encoded, and are inducible by exposure to some beta-lactam agents and resistant to inhibition by marketed beta-lactamase inhibitors. In an ongoing effort to alleviate this problem a series of novel 4-substituted trinems was designed and synthesized. Significant in vitro inhibitory activity was measured against the bacterial beta-lactamases of class C and additionally against class A. The lead compound LK-157 was shown to be a potent mechanism-based inactivator. Acylation of the active site Ser 64 of the class C enzyme beta-lactamase was observed in the solved crystal structures of two inhibitors complexes to AmpC enzyme from E. cloacae. Structure-activity relationships in the series reveal the importance of the trinem scaffold for inhibitory activity and the interesting potential of the series for further development.
    Journal of Medicinal Chemistry 09/2007; 50(17):4113-21. · 5.61 Impact Factor
  • Source
    Miha Kotnik, Petra Stefanic Anderluh, Andrej Prezelj
    [Show abstract] [Hide abstract]
    ABSTRACT: The widespread emergence of pathogenic bacterial strains with resistance to antibiotics is becoming a serious threat to public health. Continuous development of novel antibacterials therefore remains one of the biggest challenges to science and unmet needs in the clinics. The biosynthetic pathway of bacterial peptidoglycan, an essential building block of cell walls, has been well studied and appears to be a rich source of attractive enzyme targets for new antibacterials. We have therefore reviewed the intracellular part of peptidoglycan biosynthesis, including the enzymes GlmS, GlmM, GlmU for formation of UDP-GlcNAc, subsequent pentapeptide synthesis by MurA-MurF, and its connection to lipid carrier by MraY and MurG. Naturally occurring inhibitors and the development of low-molecular weight inhibitors of the intracellular part of peptidoglycan synthesis are presented.
    Current pharmaceutical design 02/2007; 13(22):2283-309. · 4.41 Impact Factor
  • Andrej Prezelj, Petra Stefanic Anderluh, Luka Peternel, Uros Urleb
    [Show abstract] [Hide abstract]
    ABSTRACT: The drawbacks and limitations of existing anticoagulant therapy which may result in serious adverse effects and a high mortality rate, have given rise to many anticoagulant development programmes in the last decade, focusing mainly at development of thrombin and FXa low-molecular weight inhibitors. A detailed understanding of blood coagulation pathways, functioning of the serine proteases thrombin, FXa, FVIIa and FIXa and elucidation of their crystal structures resulted in many potent compounds, among which some have entered the clinical phase or have been approved for use in clinical practice. Recently, the focus of anticoagulant research turned to inhibition of the TF:FVIIa complex, with some promising clinical candidates on the horizon. This article provides an overview of the current development status of serine protease inhibitors as anticoagulants, including new trends such as dual coagulation factor inhibitors.
    Current pharmaceutical design 02/2007; 13(3):287-312. · 4.41 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Closure time measured by a platelet function analyser (PFA-100) was examined for its usefulness in assessing the efficacy of platelet membrane glycoprotein IIb/IIIa antagonists in vitro, and was compared to optical platelet aggregometry. Three known glycoprotein IIb/IIIa antagonists [H-Arg-Gly-Asp-Ser-OH (RGDS), tirofiban and eptifibatide] and six new peptidomimetic glycoprotein IIb/IIIa antagonists (DKT-59, DPS-172, SMA-101, SMA-104, SMA-179 and SKN-191) were assessed. The concentration of antagonist which doubled closure time in collagen/ADP and collagen/epinephrine cartridges (IC200) or decreased ADP- or collagen-induced platelet aggregation by 50% (IC50) was used to assess the efficacy of the glycoprotein IIb/IIIa antagonist in inhibiting platelet function. IC200 for collagen/ADP and collagen/epinephrine closure times and IC50 for ADP- and collagen-induced platelet aggregation were highly associated (correlation coefficients 0.97-1.00, all p<0.001). Therefore, according to both methods, the most efficient glycoprotein IIb/IIIa antagonist was tirofiban (IC200=0.030-0.034 micromol/L, IC50=0.005-0.027 micromol/L) and the least efficient was RGDS (IC200=875-1100 micromol/L, IC50=124-377 micromol/L; all data are means), while the new peptidomimetic glycoprotein IIb/IIIa antagonists exhibited intermediate efficacies. Closure time represents a fast, simple and sensitive method of assessing glycoprotein IIb/IIIa antagonism in vitro, is comparable to optical aggregometry, and suitable for testing larger numbers of glycoprotein IIb/IIIa antagonists.
    Clinical Chemistry and Laboratory Medicine 01/2007; 45(11):1542-8. · 3.01 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: A novel class of potential antithrombotic compounds with moderate thrombin inhibitory and fibrinogen receptor antagonistic activity is described. Combination of anticoagulant and antiaggregatory activity in the same molecular entity is presented as a new promising approach in the search for novel antithrombotic agents.
    Journal of Medicinal Chemistry 06/2005; 48(9):3110-3. · 5.61 Impact Factor

Publication Stats

62 Citations
27.69 Total Impact Points


  • 2005–2009
    • University of Ljubljana
      • • Department of Chemical Technology
      • • Faculty of Pharmacy
      Lubliano, Ljubljana, Slovenia