The Experts below are selected from a list of 3771 Experts worldwide ranked by ideXlab platform
Nadine Jagerovic - One of the best experts on this subject based on the ideXlab platform.
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new pyridazinone 4 Carboxamides as new cannabinoid receptor type 2 inverse agonists synthesis pharmacological data and molecular docking
European Journal of Medicinal Chemistry, 2017Co-Authors: Giulio Ragusa, Maria Gomezcanas, Paula Morales, Carmen Rodriguezcueto, Maria Ruth Pazos, Battistina Asproni, Elena Cichero, Paola Fossa, Gerard Aime Pinna, Nadine JagerovicAbstract:In the last few years, cannabinoid type-2 receptor (CB2R) selective ligands have shown a great potential as novel therapeutic drugs in several diseases. With the aim of discovering new selective cannabinoid ligands, a series of pyridazinone-4-Carboxamides was designed and synthesized, and the new derivatives tested for their affinity toward the hCB1R and hCB2R. The 6-(4-chloro-3-methylphenyl)-2-(4-fluorobenzyl)-N-(cis-4-methylcyclohexyl)-3-oxo-2,3-dihydropyridazine-4-carboxamide (9) displayed high CB2-affinity (KiCB2 = 2.0 ± 0.81 nM) and a notable selectivity (KiCB1/KiCB2 > 2000). In addition, 9 and other active new synthesized entities have demonstrated to behave as CB2R inverse agonists in [35S]-GTPγS binding assay. ADME predictions of the newly synthesized CB2R ligands suggest a favourable pharmacokinetic profile. Docking studies disclosed the specific pattern of interactions of these derivatives. Our results support that pyridazinone-4-Carboxamides represent a new promising scaffold for the development of potent and selective CB2R ligands.
Cesur Zafer - One of the best experts on this subject based on the ideXlab platform.
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Novel N-(1-thia-4-azaspiro[4.5]decan-4-yl)carboxamide derivatives as potent and selective influenza virus fusion inhibitors
'Wiley', 2019Co-Authors: Göktaş Füsun, Vanderlinden Evelien, Naesens Lieve, Özbil Mehmet, Cesur Nesrin, Cesur ZaferAbstract:Özbil, Mehmet (Arel Author)Hemagglutinin is the surface protein of the influenza virus that mediates both binding and penetration of the virus into host cells. We here report on the synthesis and structure-activity relationship of some novel N-(1-thia-4-azaspiro[4.5]decan-4-yl)-carboxamide compounds carrying the 5-chloro-2-methoxybenzamide structure, designed as influenza virus fusion inhibitors. The Carboxamides (1a-h, 2a-h) have a similar backbone structure as the fusion inhibitors that we reported on previously. Compounds 2b and 2d displayed inhibitory activity against influenza A/H3N2 virus replication (average antiviral EC50: 2.1 mu M for 2b and 3.4 mu M for 2d). Data obtained in the hemolysis inhibition assay supported that these compounds act as inhibitors of the influenza virus hemagglutinin-mediated fusion process
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Novel N-(1-thia-4-azaspiro[4.5]decan-4-yl)carboxamide derivatives as potent and selective influenza virus fusion inhibitors
'Wiley', 2019Co-Authors: Göktaş Füsun, Vanderlinden Evelien, Naesens Lieve, Özbil Mehmet, Cesur Nesrin, Cesur ZaferAbstract:Hemagglutinin is the surface protein of the influenza virus that mediates both binding and penetration of the virus into host cells. We here report on the synthesis and structure-activity relationship of some novel N-(1-thia-4-azaspiro[4.5]decan-4-yl)-carboxamide compounds carrying the 5-chloro-2-methoxybenzamide structure, designed as influenza virus fusion inhibitors. The Carboxamides (1a-h, 2a-h) have a similar backbone structure as the fusion inhibitors that we reported on previously. Compounds 2b and 2d displayed inhibitory activity against influenza A/H3N2 virus replication (average antiviral EC50 : 2.1 µM for 2b and 3.4 µM for 2d). Data obtained in the hemolysis inhibition assay supported that these compounds act as inhibitors of the influenza virus hemagglutinin-mediated fusion process.status: publishe
Naesens Lieve - One of the best experts on this subject based on the ideXlab platform.
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Novel N-(1-thia-4-azaspiro[4.5]decan-4-yl)carboxamide derivatives as potent and selective influenza virus fusion inhibitors
'Wiley', 2019Co-Authors: Göktaş Füsun, Vanderlinden Evelien, Naesens Lieve, Özbil Mehmet, Cesur Nesrin, Cesur ZaferAbstract:Hemagglutinin is the surface protein of the influenza virus that mediates both binding and penetration of the virus into host cells. We here report on the synthesis and structure-activity relationship of some novel N-(1-thia-4-azaspiro[4.5]decan-4-yl)-carboxamide compounds carrying the 5-chloro-2-methoxybenzamide structure, designed as influenza virus fusion inhibitors. The Carboxamides (1a-h, 2a-h) have a similar backbone structure as the fusion inhibitors that we reported on previously. Compounds 2b and 2d displayed inhibitory activity against influenza A/H3N2 virus replication (average antiviral EC50 : 2.1 µM for 2b and 3.4 µM for 2d). Data obtained in the hemolysis inhibition assay supported that these compounds act as inhibitors of the influenza virus hemagglutinin-mediated fusion process.status: publishe
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Novel N-(1-thia-4-azaspiro[4.5]decan-4-yl)carboxamide derivatives as potent and selective influenza virus fusion inhibitors
'Wiley', 2019Co-Authors: Göktaş Füsun, Vanderlinden Evelien, Naesens Lieve, Özbil Mehmet, Cesur Nesrin, Cesur ZaferAbstract:Özbil, Mehmet (Arel Author)Hemagglutinin is the surface protein of the influenza virus that mediates both binding and penetration of the virus into host cells. We here report on the synthesis and structure-activity relationship of some novel N-(1-thia-4-azaspiro[4.5]decan-4-yl)-carboxamide compounds carrying the 5-chloro-2-methoxybenzamide structure, designed as influenza virus fusion inhibitors. The Carboxamides (1a-h, 2a-h) have a similar backbone structure as the fusion inhibitors that we reported on previously. Compounds 2b and 2d displayed inhibitory activity against influenza A/H3N2 virus replication (average antiviral EC50: 2.1 mu M for 2b and 3.4 mu M for 2d). Data obtained in the hemolysis inhibition assay supported that these compounds act as inhibitors of the influenza virus hemagglutinin-mediated fusion process
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Synthesis and biological evaluation of N-alkyl-3-(alkylamino)-pyrazine-2-Carboxamides
'MDPI AG', 2015Co-Authors: Semelkova Lucia, Konecna Klara, Paterova Pavla, Kubicek Vladimir, Kunes Jiri, Novakova Lucie, Marek Jan, Naesens Lieve, Pesko Matus, Kralova KatarinaAbstract:A series of N-alkyl-3-(alkylamino)pyrazine-2-Carboxamides and their N-alkyl-3-chloropyrazine-2-carboxamide precursors were prepared. All compounds were characterized by analytical methods and tested for antimicrobial and antiviral activity. The antimycobacterial MIC values against Mycobacterium tuberculosis H37Rv of the most effective compounds, 3-(hexylamino)-, 3-(heptylamino)- and 3-(octylamino)-N-methyl-pyrazine-2-Carboxamides 14‒16, was 25 μg/mL. The compounds inhibited photosystem 2 photosynthetic electron transport (PET) in spinach chloroplasts. This activity was strongly connected with the lipophilicity of the compounds. For effective PET inhibition longer alkyl chains in the 3-(alkylamino) substituent in the N-alkyl-3-(alkylamino)pyrazine-2-carboxamide molecule were more favourable than two shorter alkyl chains.status: publishe
Michael J Waring - One of the best experts on this subject based on the ideXlab platform.
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sequence specificity of the binding of 9 aminoacridine and amsacrine 4 Carboxamides to dna studied by dnase i footprinting
Biochemistry, 1992Co-Authors: William A. Denny, Laurence P. G. Wakelin, L E Mellor, Michael J WaringAbstract:: DNase I footprinting has been used to probe the sequence selectivity of binding of a series of intercalating amsacrine-4-Carboxamides and a related 9-aminoacridine-4-carboxamide to three DNA restriction fragments. These ligands have good experimental antileukemic activity, and for those members of the series that gave evaluable footprints, our principal finding is that they bind preferentially to GC-rich regions in agreement with the conclusion of equilibrium and kinetic measurements. The highest affinity sites generally occur in clusters of GC base pairs with runs of AT pairs being excluded from binding. It is important to appreciate that the 9-aminoacridine- and amsacrine-4-Carboxamides exhibit a very high degree of selectivity for GC sites which, to our knowledge, has not been previously matched by acridine derivatives in footprinting experiments. The principal determinant of specificity appears to be the 4-carboxamide group itself since neither variations in the terminal funtionality of the 4-carboxamide sidechain nor the presence of the 9-anilino substituent modifies sequence preferences. The molecular origins of selectivity may be discerned in terms of potential hydrogen bonding interactions between the 4-carboxamide moiety and carbonyl oxygen and amino groups of GC base pairs in the DNA minor groove at CG dinucleotide sites. The related therapeutic agent amsacrine failed to inhibit cleavage by DNase I, so no conclusion can be drawn concerning its binding selectivity, save to note that amsacrine does not possess the 4-carboxamide group which appears to be the crucial determinant of GC specificity. Whether selectivity for binding to GC-rich sequences is an important element in the antitumor activity of both the 9-aminoacridine- and amsacrine-4-Carboxamides remains to be determined.
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sequence specificity of the binding of 9 aminoacridine and amsacrine 4 Carboxamides to dna studied by dnase i footprinting
Biochemistry, 1992Co-Authors: William A. Denny, Laurence P. G. Wakelin, L E Mellor, Michael J WaringAbstract:DNase I footprinting has been used to probe the sequence selectivity of binding of a series of intercalating amsacrine-4-Carboxamides and a related 9-aminoacridine-4-carboxamide to three DNA restriction fragments. These ligands have good experimental antileukemic activity, and for those members of the series that gave evaluable footprints, our principal finding is that they bind preferentially to GC-rich regions in agreement with the conclusion of equilibrium and kinetic measurements. The highest affinity sites generally occur in clusters of GC base pairs with runs of AT pairs being excluded from binding
Giulio Ragusa - One of the best experts on this subject based on the ideXlab platform.
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new pyridazinone 4 Carboxamides as new cannabinoid receptor type 2 inverse agonists synthesis pharmacological data and molecular docking
European Journal of Medicinal Chemistry, 2017Co-Authors: Giulio Ragusa, Maria Gomezcanas, Paula Morales, Carmen Rodriguezcueto, Maria Ruth Pazos, Battistina Asproni, Elena Cichero, Paola Fossa, Gerard Aime Pinna, Nadine JagerovicAbstract:In the last few years, cannabinoid type-2 receptor (CB2R) selective ligands have shown a great potential as novel therapeutic drugs in several diseases. With the aim of discovering new selective cannabinoid ligands, a series of pyridazinone-4-Carboxamides was designed and synthesized, and the new derivatives tested for their affinity toward the hCB1R and hCB2R. The 6-(4-chloro-3-methylphenyl)-2-(4-fluorobenzyl)-N-(cis-4-methylcyclohexyl)-3-oxo-2,3-dihydropyridazine-4-carboxamide (9) displayed high CB2-affinity (KiCB2 = 2.0 ± 0.81 nM) and a notable selectivity (KiCB1/KiCB2 > 2000). In addition, 9 and other active new synthesized entities have demonstrated to behave as CB2R inverse agonists in [35S]-GTPγS binding assay. ADME predictions of the newly synthesized CB2R ligands suggest a favourable pharmacokinetic profile. Docking studies disclosed the specific pattern of interactions of these derivatives. Our results support that pyridazinone-4-Carboxamides represent a new promising scaffold for the development of potent and selective CB2R ligands.
