Edward T. Petri

University of Novi Sad

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Andjelka S. Ćelić

University of Novi Sad

Olivera R. Klisurić

University of Novi Sad

Sofija S. Bekić

University of Novi Sad

Marija N. Sakač

University of Novi Sad

Evgenija A. Djurendić

University of Novi Sad

Dimitar Jakimov

Oncology Institute of Vojvodina

Jovana J. Ajduković

University of Novi Sad

Marina P. Savić

University of Novi Sad

Andrea R. Nikolić

University of Novi Sad

Barbara E. Ehrlich

Yale University

Cooperative Institutions

University of Novi Sad

Yale University

Universitäts Frauenklinik

Johannes Gutenberg University Mainz

Case Western Reserve University

Heinrich Heine University Düsseldorf

University of Rochester

University of Rochester Medical Center

University of Belgrade

Heidelberg University

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

CCDC 901001: Experimental Crystal Structure Determination

The Cambridge Structural Database (2013)

Katarina Penov‐Gasi Aleksandar M. Oklješa Edward T. Petri Andjelka S. Ćelić Evgenija A. Djurendić

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

10.5517/ccz7kk9

Cite

Citations (0)

Synthesis of Camphor-Derived Bis(pyrazolylpyridine) Rhodium(III) Complexes: Structure–Reactivity Relationships and Biological Activity

Inorganic Chemistry (2018)

Angelina Petrović Milan M. Milutinović Edward T. Petri Marko Živanović Nevena Milivojević

Two novel rhodium(III) complexes, namely, [RhIII(X)Cl3] (X = 2 2,6-bis((4 S,7 R)-7,8,8-trimethyl-4,5,6,7-tetrahydro-1 H-4,7-methanoindazol-3-yl)pyridine or 2,6-bis((4 S,7 R)-1,7,8,8-tetramethyl-4,5,6,7-tetrahydro-1 H-4,7-methanoindazol-3-yl)pyridine), were synthesized from camphor derivatives of a bis(pyrazolylpyridine), tridentate nitrogen-donor chelate system, giving [RhIII(H2L*)Cl3] (1a) and [RhIII(Me2L*)Cl3] (1b). A rhodium(III) terpyridine (terpy) ligand complex, [RhIII(terpy)Cl3] (1c), was also synthesized. By single-crystal X-ray analysis, 1b crystallizes in an orthorhombic P212121 system, with two molecules in the asymmetric unit. Tridentate coordination by the N,N,N-donor localizes the central nitrogen atom close to the rhodium(III) center. Compounds 1a and 1b were reactive toward l-methionine (l-Met), guanosine-5'-monophosphate (5'-GMP), and glutathione (GSH), with an order of reactivity of 5'-GMP > GSH > l-Met. The order of reactivity of the RhIII complexes was: 1b> 1a > 1c. The RhIII complexes showed affinity for calf thymus DNA and bovine serum albumin by UV-vis and emission spectral studies. Furthermore, 1b showed significant in vitro cytotoxicity against human epithelial colorectal carcinoma cells. Since the RhIII complexes have similar coordination modes, stability differences were evaluated by density functional theory (DFT) calculations (B3LYP(CPCM)/LANL2DZp). With (H2L*) and (terpy) as model ligands, DFT calculations suggest that both tridentate ligand systems have similar stability. In addition, molecular docking suggests that all test compounds have affinity for the minor groove of DNA, while 1b and 1c have potential for DNA intercalation.

Reactivity

Orthorhombic crystal system

10.1021/acs.inorgchem.8b02390

Cite

Citations (35)

CCDC 922751: Experimental Crystal Structure Determination

The Cambridge Structural Database (2013)

Marina P. Savić Evgenija A. Djurendić Edward T. Petri Andjelka Elic Olivera R. Klisurić

10.5517/cczz659

Cite

Citations (0)

Investigation of the Potential of Bile Acid Methyl Esters as Inhibitors of Aldo‐keto Reductase 1C2: Insight from Molecular Docking, Virtual Screening, Experimental Assays and Molecular Dynamics

Molecular Informatics (2022)

Maja Marinović Edward T. Petri Ljubica Grbović Bojana Vasiljević Suzana Jovanović-Šanta

Abstract Human aldo‐keto reductase 1C isoforms (AKR1C1‐C4) catalyze reduction of endogenous and exogenous compounds, including therapeutic drugs, and are associated with chemotherapy resistance. AKR1C2 is involved in metastatic processes and is a target for the treatment of various cancers. Here we used molecular docking to explore the potential of a series of eleven bile acid methyl esters as AKR1C2 inhibitors. Autodock 4.2 ranked 10 of the 11 test compounds above a decoy set generated based on ursodeoxycholic acid, a known AKR1C2 inhibitor, while 5 of these 10 ranked above 94 % of decoys in Autodock Vina. Seven inactives reported in the literature not to inhibit AKR1C2 ranked below the decoy threshold: 5 of these are specific inhibitors of AKR1C3, a related isoform. Using the same parameters, Autodock Vina identified steroidal analogs of AKR1C substrates, bile acids, and AKR1C inhibitors in the top 5 % of a virtual screen of a natural product library. In experimental assays, 6 out of 11 of the tested bile acid methyl esters inhibited >50 % of AKR1C2 activity, while 2 compounds were strong AKR1C3 inhibitors. Potential off‐target interactions with the glucocorticoid receptor were measured using a yeast‐based fluorescence assay, where results suggest that the methyl ester could interfere with binding. The top ranking compound based on docking and experimental results showed dose‐dependent inhibition of AKR1C2 with an IC50 of ∼3.6 μM. Molecular dynamics simulations (20 ns) were used to explore potential interactions between a bile acid methyl ester and residues in the AKR1C2 active site. Our molecular docking results identify AKR1C2 as a target for bile acid methyl esters, which combined with virtual screening results could provide new directions for researchers interested in synthesis of AKR1C inhibitors.

Aldo-keto reductase

Docking (animal)

Sulforhodamine B

AutoDock

10.1002/minf.202100256

Cite

Citations (7)

Development of new steroid-based hydrazide and (thio)semicarbazone compounds with anticancer properties

The Journal of Steroid Biochemistry and Molecular Biology (2024)

Ðorđe D. Janković Tijana Lj. Šestić Sofija S. Bekić Marina P. Savić Andjelka S. Ćelić

Semicarbazone

Thio-

10.1016/j.jsbmb.2024.106545

Cite

Citations (0)

Calcium-induced Conformational Changes in C-terminal Tail of Polycystin-2 Are Necessary for Channel Gating

Journal of Biological Chemistry (2012)

Andjelka S. Ćelić Edward T. Petri Jennifer H. Benbow Michael E. Hodsdon Barbara E. Ehrlich

Polycystin-2 (PC2) is a Ca(2+)-permeable transient receptor potential channel activated and regulated by changes in cytoplasmic Ca(2+). PC2 mutations are responsible for ∼15% of autosomal dominant polycystic kidney disease. Although the C-terminal cytoplasmic tail of PC2 has been shown to contain a Ca(2+)-binding EF-hand domain, the molecular basis of PC2 channel gating by Ca(2+) remains unknown. We propose that the PC2 EF-hand is a Ca(2+) sensor required for channel gating. Consistent with this, Ca(2+) binding causes a dramatic decrease in the radius of gyration (R(g)) of the PC2 EF-hand by small angle x-ray scattering and significant conformational changes by NMR. Furthermore, increasing Ca(2+) concentrations cause the C-terminal cytoplasmic tail to transition from a mixture of extended oligomers to a single compact dimer by analytical ultracentrifugation, coupled with a >30 Å decrease in maximum interatomic distance (D(max)) by small angle x-ray scattering. Mutant PC2 channels unable to bind Ca(2+) via the EF-hand are inactive in single-channel planar lipid bilayers and inhibit Ca(2+) release from ER stores upon overexpression in cells, suggesting dominant negative properties. Our results support a model where PC2 channels are gated by discrete conformational changes in the C-terminal cytoplasmic tail in response to changes in cytoplasmic Ca(2+) levels. These properties of PC2 are lost in autosomal dominant polycystic kidney disease, emphasizing the importance of PC2 to kidney cell function. We speculate that PC2 and the Ca(2+)-dependent transient receptor potential channels in general are regulated by similar conformational changes in their cytoplasmic domains that are propagated to the channel pore.

10.1074/jbc.m112.354613

Cite

Citations (48)

CCDC 1847938: Experimental Crystal Structure Determination

The Cambridge Structural Database (2018)

Angelina Petrovic Milan M. Milutinović Edward T. Petri Marko Živanović Nevena Milivojević

10.5517/ccdc.csd.cc200xxw

Cite

Citations (0)

Discrete Proteolysis Of Neuronal Calcium Sensor 1 By μ-calpain Disrupts Calcium Binding

Biophysical Journal (2009)

Courtney Blachford Andjelka S. Ćelić Edward T. Petri Barbara E. Ehrlich

Isothermal Titration Calorimetry

Proteolysis

Cleavage (geology)

Calcium in biology

10.1016/j.bpj.2008.12.534

Cite

Citations (0)

X-ray structure of human aldo–keto reductase 1C3 in complex with a bile acid fused tetrazole inhibitor: experimental validation, molecular docking and structural analysis

RSC Medicinal Chemistry (2022)

Maja Marinović Sofija S. Bekić Michaël Kugler J. Brynda Jana Škerlová

Aldo-keto reductase 1C3 (AKR1C3) catalyzes the reduction of androstenedione to testosterone and reduces the effectiveness of chemotherapeutics. AKR1C3 is a target for treatment of breast and prostate cancer and AKR1C3 inhibition could be an effective adjuvant therapy in the context of leukemia and other cancers. In the present study, steroidal bile acid fused tetrazoles were screened for their ability to inhibit AKR1C3. Four C24 bile acids with C-ring fused tetrazoles were moderate to strong AKR1C3 inhibitors (37-88% inhibition), while B-ring fused tetrazoles had no effect on AKR1C3 activity. Based on a fluorescence assay in yeast cells, these four compounds displayed no affinity for estrogen receptor-α, or the androgen receptor, suggesting a lack of estrogenic or androgenic effects. A top inhibitor showed specificity for AKR1C3 over AKR1C2, and inhibited AKR1C3 with an IC50 of ∼7 μM. The structure of AKR1C3·NADP+ in complex with this C-ring fused bile acid tetrazole was determined by X-ray crystallography at 1.4 Å resolution, revealing that the C24 carboxylate is anchored to the catalytic oxyanion site (H117, Y55); meanwhile the tetrazole interacts with a tryptophan (W227) important for steroid recognition. Molecular docking predicts that all four top AKR1C3 inhibitors bind with nearly identical geometry, suggesting that C-ring bile acid fused tetrazoles represent a new class of AKR1C3 inhibitors.

Aldo-keto reductase

Tetrazole

Docking (animal)

10.1039/d2md00387b

Cite

Citations (7)

Analysis of the cytoplasmic interaction between polycystin-1 and polycystin-2

AJP Renal Physiology (2009)

Jozefina Casuscelli Stefan Schmidt Brenda DeGray Edward T. Petri Andjelka S. Ćelić

Autosomal dominant polycystic kidney disease (ADPKD) arises following mutations of either Pkd1 or Pkd2. The proteins these genes encode, polycystin-1 (PC1) and polycystin-2 (PC2), form a signaling complex using direct intermolecular interactions. Two distinct domains in the C-terminal tail of PC2 have recently been identified, an EF-hand and a coiled-coil domain. Here, we show that the PC2 coiled-coil domain interacts with the C-terminal tail of PC1, but that the PC2 EF-hand domain does not. We measured the K0.5 of the interaction between the C-terminal tails of PC1 and PC2 and showed that the direct interaction of these proteins is abrogated by a PC1 point mutation that was identified in ADPKD patients. Finally, we showed that overexpression of the PC1 C-terminal tail in MDCK cells alters the Ca2+ response, but that overexpression of the PC1 C-terminal tail containing the disease mutation does not. These results allow a more detailed understanding of the mechanism of pathogenic mutations in the cytoplasmic regions of PC1 and PC2.

PKD1

10.1152/ajprenal.00412.2009

Cite

Citations (38)