Mining a Cathepsin Inhibitor Library for New Antiparasitic Drug Leads
Publication Date
May 03, 2011
Journal
PLOS Neglected Tropical Diseases
Authors
Kenny K. H. Ang, Joseline Ratnam, Jiri Gut, Jennifer Legac, et al
Volume
5
Issue
5
Pages
e1023
DOI
https://dx.plos.org/10.1371/journal.pntd.0001023
Publisher URL
http://journals.plos.org/plosntds/article?id=10.1371%2Fjournal.pntd.0001023
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/21572521
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086806
Europe PMC
http://europepmc.org/abstract/MED/21572521
Web of Science
000291099100004
Scopus
79957989066
Mendeley
http://www.mendeley.com/research/mining-cathepsin-inhibitor-library-new-antiparasitic-drug-leads
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Mendeley | Further Information

{"title"=>"Mining a cathepsin inhibitor library for new antiparasitic drug leads", "type"=>"journal", "authors"=>[{"first_name"=>"Kenny K.H.", "last_name"=>"Ang", "scopus_author_id"=>"26535505700"}, {"first_name"=>"Joseline", "last_name"=>"Ratnam", "scopus_author_id"=>"26537987400"}, {"first_name"=>"Jiri", "last_name"=>"Gut", "scopus_author_id"=>"7005552723"}, {"first_name"=>"Jennifer", "last_name"=>"Legac", "scopus_author_id"=>"6506296940"}, {"first_name"=>"Elizabeth", "last_name"=>"Hansell", "scopus_author_id"=>"6603045001"}, {"first_name"=>"Zachary B.", "last_name"=>"Mackey", "scopus_author_id"=>"6603290428"}, {"first_name"=>"Katarzyna M.", "last_name"=>"Skrzypczynska", "scopus_author_id"=>"42762180700"}, {"first_name"=>"Anjan", "last_name"=>"Debnath", "scopus_author_id"=>"57195541647"}, {"first_name"=>"Juan C.", "last_name"=>"Engel", "scopus_author_id"=>"7402399288"}, {"first_name"=>"Philip J.", "last_name"=>"Rosenthal", "scopus_author_id"=>"55137938300"}, {"first_name"=>"James H.", "last_name"=>"McKerrow", "scopus_author_id"=>"35596191600"}, {"first_name"=>"Michelle R.", "last_name"=>"Arkin", "scopus_author_id"=>"6603802946"}, {"first_name"=>"Adam R.", "last_name"=>"Renslo", "scopus_author_id"=>"6603197208"}], "year"=>2011, "source"=>"PLoS Neglected Tropical Diseases", "identifiers"=>{"sgr"=>"79957989066", "pmid"=>"21572521", "scopus"=>"2-s2.0-79957989066", "pui"=>"361887719", "isbn"=>"1935-2735 (Electronic)\\n1935-2727 (Linking)", "issn"=>"19352727", "doi"=>"10.1371/journal.pntd.0001023"}, "id"=>"06247678-24a8-38c6-86fa-6b45659aeb3d", "abstract"=>"The targeting of parasite cysteine proteases with small molecules is emerging as a possible approach to treat tropical parasitic diseases such as sleeping sickness, Chagas' disease, and malaria. The homology of parasite cysteine proteases to the human cathepsins suggests that inhibitors originally developed for the latter may be a source of promising lead compounds for the former. We describe here the screening of a unique ∼ 2,100-member cathepsin inhibitor library against five parasite cysteine proteases thought to be relevant in tropical parasitic diseases. Compounds active against parasite enzymes were subsequently screened against cultured Plasmodium falciparum, Trypanosoma brucei brucei and/or Trypanosoma cruzi parasites and evaluated for cytotoxicity to mammalian cells. The end products of this effort include the identification of sub-micromolar cell-active leads as well as the elucidation of structure-activity trends that can guide further optimization efforts.", "link"=>"http://www.mendeley.com/research/mining-cathepsin-inhibitor-library-new-antiparasitic-drug-leads", "reader_count"=>51, "reader_count_by_academic_status"=>{"Unspecified"=>3, "Professor > Associate Professor"=>3, "Researcher"=>19, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>11, "Student > Postgraduate"=>1, "Other"=>3, "Student > Master"=>4, "Student > Bachelor"=>2, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>3, "Professor > Associate Professor"=>3, "Researcher"=>19, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>11, "Student > Postgraduate"=>1, "Other"=>3, "Student > Master"=>4, "Student > Bachelor"=>2, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>7, "Biochemistry, Genetics and Molecular Biology"=>2, "Agricultural and Biological Sciences"=>20, "Medicine and Dentistry"=>2, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Veterinary Science and Veterinary Medicine"=>1, "Physics and Astronomy"=>1, "Chemistry"=>14, "Social Sciences"=>1, "Computer Science"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>14}, "Social Sciences"=>{"Social Sciences"=>1}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>20}, "Computer Science"=>{"Computer Science"=>2}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Unspecified"=>{"Unspecified"=>7}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}, "Veterinary Science and Veterinary Medicine"=>{"Veterinary Science and Veterinary Medicine"=>1}}, "reader_count_by_country"=>{"Pakistan"=>1, "United States"=>1, "Uruguay"=>1, "Brazil"=>1, "United Kingdom"=>1, "Israel"=>1}, "group_count"=>3}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/777665"], "description"=>"<p>Illustrated are significantly represented chemotypes at three positions: warhead/P1, P2, and P3. Indicated in parentheses are the approximate number of library members possessing each substructural chemotype.</p>", "links"=>[], "tags"=>["cathepsin", "inhibitor"], "article_id"=>448016, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structural_composition_of_the_cathepsin_inhibitor_library_/448016", "title"=>"Structural composition of the cathepsin inhibitor library.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:39:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/777860"], "description"=>"<p>Single-point inhibition data for rhodesain (Y-axis, % inhibition at 0.1 µM test compound) as compared to other parasite enzymes (X-axes), including: (A) cruzain (% inhibition at 0.1 µM), (B) falcipain-3 (% inhibition at 0.05 µM), (C) TbCatB (% inhibition at 1 µM), and (D) trypanathione reductase (% inhibition at 10 µM). Individual data points are colored according to warhead/P1 type as follows: vinylsulfones (red), nitriles unsubstituted or monosubstituted at P1 (blue), nitriles with geminal cyclic substitution at P1 (light blue), keto-heterocycles (green), hydroxy/alkoxy ketones (yellow) and others (grey). The shape of each data point corresponds to the P2 chemotype as follows: phenylalanine (triangle), benzyl cysteine or homphenylalanine (needle); naphthalene (circle), spirocyclic (open circle), dihalogenated phenylalanine (diamond), leucine/leucine-like (square) and others (open square).</p>", "links"=>[], "tags"=>["percent", "inhibition", "compounds", "cysteine"], "article_id"=>448212, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Comparing_percent_inhibition_of_compounds_between_cysteine_proteases_/448212", "title"=>"Comparing percent inhibition of compounds between cysteine proteases.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:40:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/777973"], "description"=>"<p>IC<sub>50</sub>, (µM) against five parasite cysteine proteases as determined for library compounds that qualified as hits from the single point screens. Data points above the dashed line had no measurable IC<sub>50</sub> (i.e., IC<sub>50</sub>>25 µM). Data points are colored and shaped by chemotype, as described in <a href=\"http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0001023#pntd-0001023-g002\" target=\"_blank\">Figure 2</a>.</p>", "links"=>[], "tags"=>["percent", "inhibition"], "article_id"=>448329, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Fifty_percent_inhibition_concentrations_/448329", "title"=>"Fifty percent inhibition concentrations.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:40:49"}
  • {"files"=>["https://ndownloader.figshare.com/files/778082"], "description"=>"<p>GI<sub>50</sub> (µM) data for selected library members against cultured <i>P. falciparum</i> (W2 strain), <i>T. brucei brucei</i>, or <i>T. cruzi</i> parasites. Data points above the dotted line had no measurable GI<sub>50</sub> (i.e., GI<sub>50</sub>>25 µM). Data points are colored and shaped by chemotype as described in <a href=\"http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0001023#pntd-0001023-g002\" target=\"_blank\">Figure 2</a>. The relative area of data points reflects cytotoxicity to mammalian cell lines (larger squares demoting increasing % growth inhibition relative to a 100% inhibition control). Cytotoxicity evaluations were performed in Jurkat cells for the <i>T. brucei</i> and <i>P. falciparum</i> actives (at 10 µM test compound) and in BESM cells for the <i>T. cruzi</i> actives (at 20 test µM compound).</p>", "links"=>[], "tags"=>["inhibition"], "article_id"=>448437, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Growth_inhibition_of_parasites_/448437", "title"=>"Growth inhibition of parasites.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:41:21"}
  • {"files"=>["https://ndownloader.figshare.com/files/778179"], "description"=>"<p>Chemical structures of protease inhibitors discussed in the text. Associated enzyme inhibition and growth inhibition data is provided in <a href=\"http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0001023#pntd-0001023-t002\" target=\"_blank\">tables 2</a>–<a href=\"http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0001023#pntd-0001023-t003\" target=\"_blank\"></a><a href=\"http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0001023#pntd-0001023-t004\" target=\"_blank\">4</a>.</p>", "links"=>[], "tags"=>["chemistry", "microbiology", "Biochemistry"], "article_id"=>448534, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Anti_plasmodium_lead_compounds_/448534", "title"=>"Anti-plasmodium lead compounds.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:41:48"}
  • {"files"=>["https://ndownloader.figshare.com/files/778305"], "description"=>"<p>Chemical structures of protease inhibitors discussed in the text. Associated enzyme inhibition and growth inhibition data is provided in <a href=\"http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0001023#pntd-0001023-t004\" target=\"_blank\">tables 4</a>–<a href=\"http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0001023#pntd-0001023-t005\" target=\"_blank\">5</a>.</p>", "links"=>[], "tags"=>["chemistry", "microbiology", "Biochemistry"], "article_id"=>448662, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.g006"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Anti_trypanosomal_lead_compounds_/448662", "title"=>"Anti-trypanosomal lead compounds.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:42:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/778428"], "description"=>"<p>Representative fluorescent images acquired with the IN Cell Analyzer 2000, taken with 20× objective magnification at Ex 350 nm/Em 460 nm, showing the host BESM nuclei (red outline) and surrounding smaller <i>T. cruzi</i> kinetoplastids (blue outline). (A) 1% DMSO as 0% inhibition control; (B) compound <b>24</b> at the highest assay concentration of 20 µM; (C) GI<sub>50</sub> dose response plots of compound <b>24</b> against <i>T. cruzi</i> and cytotoxicity to host BESM cells.</p>", "links"=>[], "tags"=>["inhibition", "compounds"], "article_id"=>448787, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.g007"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_T_cruzi_growth_inhibition_of_compounds_24_/448787", "title"=>"<i>T. cruzi</i> growth inhibition of compounds 24.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:43:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/778522"], "description"=>"<p>Effects of pre-incubation time on falcipain-3 IC<sub>50</sub> values for inhibitors of different chemotype.</p>", "links"=>[], "tags"=>["pre-incubation", "falcipain-3", "inhibitors"], "article_id"=>448879, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.t001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effects_of_pre_incubation_time_on_falcipain_3_IC_50_values_for_inhibitors_of_different_chemotype_/448879", "title"=>"Effects of pre-incubation time on falcipain-3 IC<sub>50</sub> values for inhibitors of different chemotype.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 18:43:44"}
  • {"files"=>["https://ndownloader.figshare.com/files/778555"], "description"=>"<p>Selected anti-plasmodium lead compounds with associated biochemical and cell-based assay data.</p>", "links"=>[], "tags"=>["anti-plasmodium", "compounds", "biochemical", "cell-based", "assay"], "article_id"=>448910, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.t002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Selected_anti_plasmodium_lead_compounds_with_associated_biochemical_and_cell_based_assay_data_/448910", "title"=>"Selected anti-plasmodium lead compounds with associated biochemical and cell-based assay data.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 18:43:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/778605"], "description"=>"<p>Selected anti-plasmodium lead compounds with associated enzyme and cell-based data.</p>", "links"=>[], "tags"=>["anti-plasmodium", "compounds", "enzyme", "cell-based"], "article_id"=>448967, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.t003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Selected_anti_plasmodium_lead_compounds_with_associated_enzyme_and_cell_based_data_/448967", "title"=>"Selected anti-plasmodium lead compounds with associated enzyme and cell-based data.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 18:44:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/778654"], "description"=>"<p>Selected anti-plasmodium lead compounds with associated enzyme and cell-based data.</p>", "links"=>[], "tags"=>["anti-plasmodium", "compounds", "enzyme", "cell-based"], "article_id"=>449010, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.t004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Selected_anti_plasmodium_lead_compounds_with_associated_enzyme_and_cell_based_data_/449010", "title"=>"Selected anti-plasmodium lead compounds with associated enzyme and cell-based data.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 18:44:29"}
  • {"files"=>["https://ndownloader.figshare.com/files/778696"], "description"=>"<p>Selected anti-trypanosomal lead compounds with associated enzyme and cell-based data.</p>", "links"=>[], "tags"=>["anti-trypanosomal", "compounds", "enzyme", "cell-based"], "article_id"=>449055, "categories"=>["Biochemistry", "Chemistry", "Microbiology"], "users"=>["Kenny K. H. Ang", "Joseline Ratnam", "Jiri Gut", "Jennifer Legac", "Elizabeth Hansell", "Zachary B. Mackey", "Katarzyna M. Skrzypczynska", "Anjan Debnath", "Juan C. Engel", "Philip J. Rosenthal", "James H. McKerrow", "Michelle R. Arkin", "Adam R. Renslo"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0001023.t005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Selected_anti_trypanosomal_lead_compounds_with_associated_enzyme_and_cell_based_data_/449055", "title"=>"Selected anti-trypanosomal lead compounds with associated enzyme and cell-based data.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 18:44:44"}

PMC Usage Stats | Further Information

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Relative Metric

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