New tetromycin derivatives with anti-trypanosomal and protease inhibitory activities.
Identifieur interne : 001449 ( PubMed/Corpus ); précédent : 001448; suivant : 001450New tetromycin derivatives with anti-trypanosomal and protease inhibitory activities.
Auteurs : Sheila M. Pimentel-Elardo ; Verena Buback ; Tobias A M. Gulder ; Tim S. Bugni ; Jason Reppart ; Gerhard Bringmann ; Chris M. Ireland ; Tanja Schirmeister ; Ute HentschelSource :
- Marine drugs [ 1660-3397 ] ; 2011.
English descriptors
- KwdEn :
- Animals, Antiprotozoal Agents (isolation & purification), Antiprotozoal Agents (pharmacology), Axinella (microbiology), Cathepsin B (antagonists & inhibitors), Cathepsin L (antagonists & inhibitors), Cysteine Endopeptidases (drug effects), Heterocyclic Compounds, 4 or More Rings (isolation & purification), Heterocyclic Compounds, 4 or More Rings (pharmacology), Leishmania major (drug effects), Magnetic Resonance Spectroscopy, Protease Inhibitors (isolation & purification), Protease Inhibitors (pharmacology), SARS Virus (drug effects), Streptomyces (chemistry), Trypanocidal Agents (isolation & purification), Trypanocidal Agents (pharmacology), Trypanosoma brucei brucei (drug effects), Viral Proteins (antagonists & inhibitors).
- MESH :
- chemical , antagonists & inhibitors : Cathepsin B, Cathepsin L, Viral Proteins.
- chemical , drug effects : Cysteine Endopeptidases.
- chemical , isolation & purification : Antiprotozoal Agents, Heterocyclic Compounds, 4 or More Rings, Protease Inhibitors, Trypanocidal Agents.
- chemical , pharmacology : Antiprotozoal Agents, Heterocyclic Compounds, 4 or More Rings, Protease Inhibitors, Trypanocidal Agents.
- chemistry : Streptomyces.
- drug effects : Leishmania major, SARS Virus, Trypanosoma brucei brucei.
- microbiology : Axinella.
- Animals, Magnetic Resonance Spectroscopy.
Abstract
Four new tetromycin derivatives, tetromycins 1-4 and a previously known one, tetromycin B (5) were isolated from Streptomyces axinellae Pol001(T) cultivated from the Mediterranean sponge Axinella polypoides. Structures were assigned using extensive 1D and 2D NMR spectroscopy as well as HRESIMS analysis. The compounds were tested for antiparasitic activities against Leishmania major and Trypanosoma brucei, and for protease inhibition against several cysteine proteases such as falcipain, rhodesain, cathepsin L, cathepsin B, and viral proteases SARS-CoV M(pro), and PL(pro). The compounds showed antiparasitic activities against T. brucei and time-dependent inhibition of cathepsin L-like proteases with K(i) values in the low micromolar range.
DOI: 10.3390/md9101682
PubMed: 22072992
Links to Exploration step
pubmed:22072992Le document en format XML
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<affiliation><nlm:affiliation>Julius-von-Sachs Institute for Biological Sciences, University of Würzburg, Julius-von-Sachs-Platz 3, Würzburg 97082, Germany. elardos@mcmaster.ca</nlm:affiliation>
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<term>Axinella (microbiology)</term>
<term>Cathepsin B (antagonists & inhibitors)</term>
<term>Cathepsin L (antagonists & inhibitors)</term>
<term>Cysteine Endopeptidases (drug effects)</term>
<term>Heterocyclic Compounds, 4 or More Rings (isolation & purification)</term>
<term>Heterocyclic Compounds, 4 or More Rings (pharmacology)</term>
<term>Leishmania major (drug effects)</term>
<term>Magnetic Resonance Spectroscopy</term>
<term>Protease Inhibitors (isolation & purification)</term>
<term>Protease Inhibitors (pharmacology)</term>
<term>SARS Virus (drug effects)</term>
<term>Streptomyces (chemistry)</term>
<term>Trypanocidal Agents (isolation & purification)</term>
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<term>Trypanosoma brucei brucei (drug effects)</term>
<term>Viral Proteins (antagonists & inhibitors)</term>
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<term>Heterocyclic Compounds, 4 or More Rings</term>
<term>Protease Inhibitors</term>
<term>Trypanocidal Agents</term>
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<term>Heterocyclic Compounds, 4 or More Rings</term>
<term>Protease Inhibitors</term>
<term>Trypanocidal Agents</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Streptomyces</term>
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<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Leishmania major</term>
<term>SARS Virus</term>
<term>Trypanosoma brucei brucei</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Axinella</term>
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<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Magnetic Resonance Spectroscopy</term>
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<front><div type="abstract" xml:lang="en">Four new tetromycin derivatives, tetromycins 1-4 and a previously known one, tetromycin B (5) were isolated from Streptomyces axinellae Pol001(T) cultivated from the Mediterranean sponge Axinella polypoides. Structures were assigned using extensive 1D and 2D NMR spectroscopy as well as HRESIMS analysis. The compounds were tested for antiparasitic activities against Leishmania major and Trypanosoma brucei, and for protease inhibition against several cysteine proteases such as falcipain, rhodesain, cathepsin L, cathepsin B, and viral proteases SARS-CoV M(pro), and PL(pro). The compounds showed antiparasitic activities against T. brucei and time-dependent inhibition of cathepsin L-like proteases with K(i) values in the low micromolar range.</div>
</front>
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<ArticleTitle>New tetromycin derivatives with anti-trypanosomal and protease inhibitory activities.</ArticleTitle>
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<Abstract><AbstractText>Four new tetromycin derivatives, tetromycins 1-4 and a previously known one, tetromycin B (5) were isolated from Streptomyces axinellae Pol001(T) cultivated from the Mediterranean sponge Axinella polypoides. Structures were assigned using extensive 1D and 2D NMR spectroscopy as well as HRESIMS analysis. The compounds were tested for antiparasitic activities against Leishmania major and Trypanosoma brucei, and for protease inhibition against several cysteine proteases such as falcipain, rhodesain, cathepsin L, cathepsin B, and viral proteases SARS-CoV M(pro), and PL(pro). The compounds showed antiparasitic activities against T. brucei and time-dependent inhibition of cathepsin L-like proteases with K(i) values in the low micromolar range.</AbstractText>
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<ForeName>Sheila M</ForeName>
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<AffiliationInfo><Affiliation>Julius-von-Sachs Institute for Biological Sciences, University of Würzburg, Julius-von-Sachs-Platz 3, Würzburg 97082, Germany. elardos@mcmaster.ca</Affiliation>
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<Author ValidYN="Y"><LastName>Reppart</LastName>
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<Author ValidYN="Y"><LastName>Schirmeister</LastName>
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<Keyword MajorTopicYN="N">anti-trypanosomal</Keyword>
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