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  1. Article ; Online: Curvicollide D Isolated from the Fungus

    Ortiz-Gonzalez, Matilde / Pérez-Victoria, Ignacio / Ramirez-Macias, Inmaculada / de Pedro, Nuria / Linde-Rodriguez, Angel / González-Menéndez, Víctor / Sanchez-Martin, Victoria / Martín, Jesús / Soriano-Lerma, Ana / Genilloud, Olga / Perez-Carrasco, Virginia / Vicente, Francisca / Maceira, José / Rodrígues-Poveda, Carlos A / Navarro-Marí, José María / Reyes, Fernando / Soriano, Miguel / Garcia-Salcedo, Jose A

    International journal of molecular sciences

    2022  Volume 23, Issue 11

    Abstract: Sleeping sickness or African trypanosomiasis is a serious health concern with an added socio-economic impact in sub-Saharan Africa due to direct infection in both humans and their domestic livestock. There is no vaccine available against African ... ...

    Abstract Sleeping sickness or African trypanosomiasis is a serious health concern with an added socio-economic impact in sub-Saharan Africa due to direct infection in both humans and their domestic livestock. There is no vaccine available against African trypanosomes and its treatment relies only on chemotherapy. Although the current drugs are effective, most of them are far from the modern concept of a drug in terms of toxicity, specificity and therapeutic regime. In a search for new molecules with trypanocidal activity, a high throughput screening of 2000 microbial extracts was performed. Fractionation of one of these extracts, belonging to a culture of the fungus
    MeSH term(s) Animals ; Fungi ; Humans ; Trypanocidal Agents/chemistry ; Trypanocidal Agents/pharmacology ; Trypanosoma brucei brucei ; Trypanosomiasis, African/drug therapy
    Chemical Substances Trypanocidal Agents
    Language English
    Publishing date 2022-05-29
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms23116107
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: 2-alkylaminoethyl-1,1-bisphosphonic acids are potent inhibitors of the enzymatic activity of Trypanosoma cruzi squalene synthase.

    Rodrígues-Poveda, Carlos A / González-Pacanowska, Dolores / Szajnman, Sergio H / Rodríguez, Juan B

    Antimicrobial agents and chemotherapy

    2012  Volume 56, Issue 8, Page(s) 4483–4486

    Abstract: As part of our efforts aimed at searching for new antiparasitic agents, the effect of representative 2-alkylaminoethyl-1,1-bisphosphonic acids on Trypanosoma cruzi squalene synthase (TcSQS) was investigated. These compounds had proven to be potent ... ...

    Abstract As part of our efforts aimed at searching for new antiparasitic agents, the effect of representative 2-alkylaminoethyl-1,1-bisphosphonic acids on Trypanosoma cruzi squalene synthase (TcSQS) was investigated. These compounds had proven to be potent inhibitors of T. cruzi. This cellular activity had been associated with an inhibition of the enzymatic activity of T. cruzi farnesyl diphosphate synthase. 2-Alkylaminoethyl-1,1-bisphosphonic acids appear to have a dual action, since they also inhibit TcSQS at the nanomolar range.
    MeSH term(s) Antiparasitic Agents/chemistry ; Antiparasitic Agents/metabolism ; Antiparasitic Agents/pharmacology ; Chagas Disease/drug therapy ; Diphosphonates/chemistry ; Diphosphonates/metabolism ; Diphosphonates/pharmacology ; Farnesyl-Diphosphate Farnesyltransferase/antagonists & inhibitors ; Farnesyl-Diphosphate Farnesyltransferase/metabolism ; Geranyltranstransferase/antagonists & inhibitors ; Parasitic Sensitivity Tests ; Structure-Activity Relationship ; Trypanocidal Agents/chemistry ; Trypanocidal Agents/metabolism ; Trypanocidal Agents/pharmacology ; Trypanosoma cruzi/drug effects ; Trypanosoma cruzi/enzymology ; Trypanosoma cruzi/metabolism
    Chemical Substances Antiparasitic Agents ; Diphosphonates ; Trypanocidal Agents ; Geranyltranstransferase (EC 2.5.1.10) ; Farnesyl-Diphosphate Farnesyltransferase (EC 2.5.1.21)
    Language English
    Publishing date 2012-05-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 217602-6
    ISSN 1098-6596 ; 0066-4804
    ISSN (online) 1098-6596
    ISSN 0066-4804
    DOI 10.1128/AAC.00796-12
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Kinetic analyses and inhibition studies reveal novel features in peptide deformylase 1 from Trypanosoma cruzi.

    Rodrígues-Poveda, Carlos A / Pérez-Moreno, Guiomar / Vidal, Antonio E / Urbina, Julio A / González-Pacanowska, Dolores / Ruiz-Pérez, Luis M

    Molecular and biochemical parasitology

    2012  Volume 182, Issue 1-2, Page(s) 83–87

    Abstract: In eubacteria and eukaryotic organelles N-terminal methionine excision requires the sequential action of two activities, a peptide deformylase (PDF), which systematically removes the N-formyl group present on all nascent polypeptides and methionine ... ...

    Abstract In eubacteria and eukaryotic organelles N-terminal methionine excision requires the sequential action of two activities, a peptide deformylase (PDF), which systematically removes the N-formyl group present on all nascent polypeptides and methionine aminopeptidase (MAP), which exscinds methionine specifically and depends on the previous removal of the N-formyl group. In Trypanosoma cruzi two genes encoding bacterial PDF homologues have been identified and referred to as TcPDF-1 and TcPDF-2. Here we report the biochemical characterization of a truncated soluble version of TcPDF-1 lacking the hydrophobic N-terminal domain that is active with the bacterial PDF substrate formyl-methionyl-alanyl-serine but, in contrast to other PDFs, is not inhibited by actinonin. The enzyme is strongly activated by Cu(2+) and inhibited by Ni(2+). Our results show that T. cruzi PDF exhibits unique features thus providing a new avenue for the design of potential inhibitors for use in the treatment of diseases caused by trypanosomatid parasites.
    MeSH term(s) Amidohydrolases/chemistry ; Amidohydrolases/genetics ; Amidohydrolases/isolation & purification ; Amino Acid Sequence ; Aminopeptidases/chemistry ; Chelating Agents/pharmacology ; Copper/pharmacology ; Culture Media ; Enzyme Activation ; Enzyme Assays ; Enzyme Inhibitors/pharmacology ; Escherichia coli/chemistry ; Escherichia coli/genetics ; Hydrophobic and Hydrophilic Interactions ; Hydroxamic Acids/pharmacology ; Kinetics ; Methionyl Aminopeptidases ; Molecular Sequence Data ; Nickel/pharmacology ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Sequence Alignment ; Solubility ; Substrate Specificity ; Trypanosoma cruzi/enzymology ; Trypanosoma cruzi/genetics
    Chemical Substances Chelating Agents ; Culture Media ; Enzyme Inhibitors ; Hydroxamic Acids ; Protozoan Proteins ; Recombinant Proteins ; Copper (789U1901C5) ; Nickel (7OV03QG267) ; Aminopeptidases (EC 3.4.11.-) ; Methionyl Aminopeptidases (EC 3.4.11.18) ; Amidohydrolases (EC 3.5.-) ; peptide deformylase (EC 3.5.1.88) ; actinonin (P18SPA8N0K)
    Language English
    Publishing date 2012-03
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 756166-0
    ISSN 1872-9428 ; 0166-6851
    ISSN (online) 1872-9428
    ISSN 0166-6851
    DOI 10.1016/j.molbiopara.2011.12.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Kinetic analyses and inhibition studies reveal novel features in peptide deformylase 1 from Trypanosoma cruzi

    Rodrígues-Poveda, Carlos A / Pérez-Moreno, Guiomar / Vidal, Antonio E / Urbina, Julio A / González-Pacanowska, Dolores / Ruiz-Pérez, Luis M

    Molecular and biochemical parasitology. 2012 , v. 182, no. 1-2

    2012  

    Abstract: In eubacteria and eukaryotic organelles N-terminal methionine excision requires the sequential action of two activities, a peptide deformylase (PDF), which systematically removes the N-formyl group present on all nascent polypeptides and methionine ... ...

    Abstract In eubacteria and eukaryotic organelles N-terminal methionine excision requires the sequential action of two activities, a peptide deformylase (PDF), which systematically removes the N-formyl group present on all nascent polypeptides and methionine aminopeptidase (MAP), which exscinds methionine specifically and depends on the previous removal of the N-formyl group. In Trypanosoma cruzi two genes encoding bacterial PDF homologues have been identified and referred to as TcPDF-1 and TcPDF-2. Here we report the biochemical characterization of a truncated soluble version of TcPDF-1 lacking the hydrophobic N-terminal domain that is active with the bacterial PDF substrate formyl-methionyl-alanyl-serine but, in contrast to other PDFs, is not inhibited by actinonin. The enzyme is strongly activated by Cu²⁺ and inhibited by Ni²⁺. Our results show that T. cruzi PDF exhibits unique features thus providing a new avenue for the design of potential inhibitors for use in the treatment of diseases caused by trypanosomatid parasites.
    Keywords Trypanosoma cruzi ; amide hydrolases ; aminopeptidases ; copper ; genes ; hydrophobicity ; methionine ; nickel ; organelles ; parasites ; parasitology ; polypeptides
    Language English
    Dates of publication 2012-03
    Size p. 83-87.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 756166-0
    ISSN 1872-9428 ; 0166-6851
    ISSN (online) 1872-9428
    ISSN 0166-6851
    DOI 10.1016/j.molbiopara.2011.12.003
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: Phosphonosulfonates are potent, selective inhibitors of dehydrosqualene synthase and staphyloxanthin biosynthesis in Staphylococcus aureus.

    Song, Yongcheng / Lin, Fu-Yang / Yin, Fenglin / Hensler, Mary / Rodrígues Poveda, Carlos A / Mukkamala, Dushyant / Cao, Rong / Wang, Hong / Morita, Craig T / González Pacanowska, Dolores / Nizet, Victor / Oldfield, Eric

    Journal of medicinal chemistry

    2008  Volume 52, Issue 4, Page(s) 976–988

    Abstract: Staphylococcus aureus produces a golden carotenoid virulence factor called staphyloxanthin (STX), and we report here the inhibition of the enzyme, dehydrosqualene synthase (CrtM), responsible for the first committed step in STX biosynthesis. The most ... ...

    Abstract Staphylococcus aureus produces a golden carotenoid virulence factor called staphyloxanthin (STX), and we report here the inhibition of the enzyme, dehydrosqualene synthase (CrtM), responsible for the first committed step in STX biosynthesis. The most active compounds are halogen-substituted phosphonosulfonates, with K(i) values as low as 5 nM against the enzyme and IC(50) values for STX inhibition in S. aureus as low as 11 nM. There is, however, only a poor correlation (R(2) = 0.27) between enzyme and cell pIC(50) (= -log(10) IC(50)) values. The ability to predict cell from enzyme data improves considerably (to R(2) = 0.72) with addition of two more descriptors. We also investigated the activity of these compounds against human squalene synthase (SQS), as a counterscreen, finding several potent STX biosynthesis inhibitors with essentially no squalene synthase activity. These results open up the way to developing potent and selective inhibitors of an important virulence factor in S. aureus, a major human pathogen.
    MeSH term(s) Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Enzyme Inhibitors ; Farnesyl-Diphosphate Farnesyltransferase/antagonists & inhibitors ; Humans ; Inhibitory Concentration 50 ; Staphylococcus aureus/drug effects ; Staphylococcus aureus/enzymology ; Staphylococcus aureus/metabolism ; Sulfonic Acids/chemistry ; Sulfonic Acids/pharmacology ; Xanthophylls/biosynthesis
    Chemical Substances Anti-Bacterial Agents ; Enzyme Inhibitors ; Sulfonic Acids ; Xanthophylls ; staphyloxanthin (71869-01-7) ; Farnesyl-Diphosphate Farnesyltransferase (EC 2.5.1.21)
    Language English
    Publishing date 2008-11-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/jm801023u
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.B 151: Show issues Location:
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  6. Article ; Online: Squalene synthase as a target for Chagas disease therapeutics.

    Shang, Na / Li, Qian / Ko, Tzu-Ping / Chan, Hsiu-Chien / Li, Jikun / Zheng, Yingying / Huang, Chun-Hsiang / Ren, Feifei / Chen, Chun-Chi / Zhu, Zhen / Galizzi, Melina / Li, Zhu-Hong / Rodrigues-Poveda, Carlos A / Gonzalez-Pacanowska, Dolores / Veiga-Santos, Phercyles / de Carvalho, Tecia Maria Ulisses / de Souza, Wanderley / Urbina, Julio A / Wang, Andrew H-J /
    Docampo, Roberto / Li, Kai / Liu, Yi-Liang / Oldfield, Eric / Guo, Rey-Ting

    PLoS pathogens

    2014  Volume 10, Issue 5, Page(s) e1004114

    Abstract: Trypanosomatid parasites are the causative agents of many neglected tropical diseases and there is currently considerable interest in targeting endogenous sterol biosynthesis in these organisms as a route to the development of novel anti-infective drugs. ...

    Abstract Trypanosomatid parasites are the causative agents of many neglected tropical diseases and there is currently considerable interest in targeting endogenous sterol biosynthesis in these organisms as a route to the development of novel anti-infective drugs. Here, we report the first x-ray crystallographic structures of the enzyme squalene synthase (SQS) from a trypanosomatid parasite, Trypanosoma cruzi, the causative agent of Chagas disease. We obtained five structures of T. cruzi SQS and eight structures of human SQS with four classes of inhibitors: the substrate-analog S-thiolo-farnesyl diphosphate, the quinuclidines E5700 and ER119884, several lipophilic bisphosphonates, and the thiocyanate WC-9, with the structures of the two very potent quinuclidines suggesting strategies for selective inhibitor development. We also show that the lipophilic bisphosphonates have low nM activity against T. cruzi and inhibit endogenous sterol biosynthesis and that E5700 acts synergistically with the azole drug, posaconazole. The determination of the structures of trypanosomatid and human SQS enzymes with a diverse set of inhibitors active in cells provides insights into SQS inhibition, of interest in the context of the development of drugs against Chagas disease.
    MeSH term(s) Animals ; Chagas Disease/drug therapy ; Chlorocebus aethiops ; Crystallography, X-Ray ; Diphosphonates/chemistry ; Diphosphonates/metabolism ; Diphosphonates/pharmacology ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/metabolism ; Enzyme Inhibitors/pharmacology ; Enzyme Inhibitors/therapeutic use ; Farnesyl-Diphosphate Farnesyltransferase/antagonists & inhibitors ; Farnesyl-Diphosphate Farnesyltransferase/chemistry ; Farnesyl-Diphosphate Farnesyltransferase/metabolism ; Humans ; Models, Molecular ; Molecular Targeted Therapy/methods ; Polyisoprenyl Phosphates/chemistry ; Polyisoprenyl Phosphates/metabolism ; Protein Binding ; Quinuclidines/chemistry ; Quinuclidines/metabolism ; Quinuclidines/pharmacology ; Sesquiterpenes/chemistry ; Sesquiterpenes/metabolism ; Trypanocidal Agents/chemistry ; Trypanocidal Agents/metabolism ; Trypanocidal Agents/pharmacology ; Trypanocidal Agents/therapeutic use ; Trypanosoma cruzi/enzymology ; Vero Cells
    Chemical Substances Diphosphonates ; Enzyme Inhibitors ; Polyisoprenyl Phosphates ; Quinuclidines ; Sesquiterpenes ; Trypanocidal Agents ; farnesyl pyrophosphate (79W6B01D07) ; Farnesyl-Diphosphate Farnesyltransferase (EC 2.5.1.21)
    Language English
    Publishing date 2014-05-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7366
    ISSN (online) 1553-7374
    ISSN 1553-7366
    DOI 10.1371/journal.ppat.1004114
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Kinetic analyses and inhibition studies reveal novel features in peptide deformylase 1 from Trypanosoma cruzi

    Rodrígues-Poveda, Carlos A. / Pérez-Moreno, Guiomar / Vidal, Antonio E. / Urbina, Julio A. / González-Pacanowska, Dolores / Ruiz-Pérez, Luis M.

    Molecular and biochemical parasitology

    Volume v. 182,, Issue no. 1

    Abstract: In eubacteria and eukaryotic organelles N-terminal methionine excision requires the sequential action of two activities, a peptide deformylase (PDF), which systematically removes the N-formyl group present on all nascent polypeptides and methionine ... ...

    Abstract In eubacteria and eukaryotic organelles N-terminal methionine excision requires the sequential action of two activities, a peptide deformylase (PDF), which systematically removes the N-formyl group present on all nascent polypeptides and methionine aminopeptidase (MAP), which exscinds methionine specifically and depends on the previous removal of the N-formyl group. In Trypanosoma cruzi two genes encoding bacterial PDF homologues have been identified and referred to as TcPDF-1 and TcPDF-2. Here we report the biochemical characterization of a truncated soluble version of TcPDF-1 lacking the hydrophobic N-terminal domain that is active with the bacterial PDF substrate formyl-methionyl-alanyl-serine but, in contrast to other PDFs, is not inhibited by actinonin. The enzyme is strongly activated by Cu²⁺ and inhibited by Ni²⁺. Our results show that T. cruzi PDF exhibits unique features thus providing a new avenue for the design of potential inhibitors for use in the treatment of diseases caused by trypanosomatid parasites.
    Keywords Trypanosoma cruzi ; aminopeptidases ; parasites ; parasitology ; copper ; methionine ; genes ; organelles ; nickel ; amide hydrolases ; polypeptides ; hydrophobicity
    Language English
    Document type Article
    ISSN 0166-6851
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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