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Start Over Author "Saccoliti F" Journal european journal of medicinal chemistry
3 results on '"Saccoliti F"'

1. Discovery of N-aryl-naphthylamines as in vitro inhibitors of the interaction between HIV integrase and the cofactor LEDGF/p75

Author

Francesco Saccoliti, Luigi Scipione, Giuliana Cuzzucoli Crucitti, Ettore Novellino, Francesco Saverio Di Leva, Luca Pescatori, Silvano Tortorella, Zeger Debyser, Sandro Cosconati, Giovanni Pupo, Antonella Messore, Valentina Noemi Madia, Roberta Costi, Roberto Di Santo, Frauke Christ, Cuzzucoli Crucitti, G, Pescatori, L, Messore, A, Madia, Vn, Pupo, G, Saccoliti, F, Scipione, L, Tortorella, S, Di Leva, F, Cosconati, Sandro, Novellino, E, Debyser, Z, Christ, F, Costi, R, Di Santo, R., Cuzzucoli Crucitti, Giuliana, Pescatori, Luca, Messore, Antonella, Madia, Valentina Noemi, Pupo, Giovanni, Saccoliti, Francesco, Scipione, Luigi, Tortorella, Silvano, Di Leva, Francesco Saverio, Novellino, Ettore, Debyser, Zeger, Christ, Frauke, Costi, Roberta, and Di Santo, Roberto

Subjects
LEDGINs, Models, Molecular, Molecular model, Stereochemistry, Plasma protein binding, HIV Integrase, Integrase, N-aryl-naphthylamine, Cofactor, Structure-Activity Relationship, para-Aminobenzoate, LEDGF/p75, Drug Discovery, Intercellular Signaling Peptides and Protein, Tumor Cells, Cultured, para-Aminobenzoates, Structure–activity relationship, Humans, LEDGIN, HIV Integrase Inhibitors, Pharmacology, biology, Dose-Response Relationship, Drug, Molecular Structure, Chemistry, Drug discovery, Drug Discovery3003 Pharmaceutical Science, Organic Chemistry, General Medicine, Small molecule, In vitro, HIV Integrase Inhibitor, integrase, drug discovery3003 pharmaceutical science, organic chemistry, pharmacology, 1-Naphthylamine, biology.protein, Intercellular Signaling Peptides and Proteins, Human, Protein Binding
Abstract

A series of N-aryl-naphthylamines, exemplified by the structures 11-16, were chosen for an in-house library screening to assay their ability to disrupt the interaction between the LEDGF cofactor and the HIV integrase. Structure modification led also to design and synthesize new compounds 17a-f. Compounds 11e,h,k,n, 13b, and 14 showed good activity in AlphaScreen assay. The most active compound 11e (IC50 Combining double low line 2.5 μM) was selected for molecular modeling studies and showed a binding mode similar to the one of the known LEDGIN 8.

Published
2015

2. Biological evaluation and structure-activity relationships of imidazole-based compounds as antiprotozoal agents.

Author

Saccoliti F, Madia VN, Tudino V, De Leo A, Pescatori L, Messore A, De Vita D, Scipione L, Brun R, Kaiser M, Mäser P, Calvet CM, Jennings GK, Podust LM, Costi R, and Di Santo R

Subjects
Animals, Antiprotozoal Agents chemical synthesis, Antiprotozoal Agents therapeutic use, Cell Line, Female, Humans, Imidazoles chemical synthesis, Imidazoles therapeutic use, Inhibitory Concentration 50, Leishmania donovani drug effects, Leishmaniasis, Visceral drug therapy, Malaria, Falciparum drug therapy, Mice, Mice, Inbred BALB C, Parasitic Sensitivity Tests, Plasmodium falciparum drug effects, Rats, Structure-Activity Relationship, Trypanosoma brucei rhodesiense drug effects, Trypanosomiasis, African drug therapy, Antiprotozoal Agents chemistry, Antiprotozoal Agents pharmacology, Chagas Disease drug therapy, Imidazoles chemistry, Imidazoles pharmacology, Trypanosoma cruzi drug effects
Abstract

We discovered a series of azole antifungal compounds as effective antiprotozoal agents. They displayed promising inhibitory activities within the micromolar-submicromolar range against P. falciparum, L. donovani, and T. b. rhodesiense. Moreover, most of such compounds showed excellent nanomolar IC 50 against T. cruzi, showing also very low cytotoxicity. Discussion of structure-activity relationships and biological data for these compounds are provided against the different parasites. To assess the mechanism of action against T. cruzi we proved that the most potent compounds (3b, 3j-l) inhibited the T. cruzi CYP51. Moreover, the most active derivative 3j dramatically reduced parasitemia in T. cruzi mouse model without acute toxicity., (Copyright © 2018 Elsevier Masson SAS. All rights reserved.)

Published
2018
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3. Discovery of N-aryl-naphthylamines as in vitro inhibitors of the interaction between HIV integrase and the cofactor LEDGF/p75.

Author

Cuzzucoli Crucitti G, Pescatori L, Messore A, Madia VN, Pupo G, Saccoliti F, Scipione L, Tortorella S, Di Leva FS, Cosconati S, Novellino E, Debyser Z, Christ F, Costi R, and Di Santo R

Subjects
1-Naphthylamine chemical synthesis, 1-Naphthylamine chemistry, 1-Naphthylamine pharmacology, Dose-Response Relationship, Drug, HIV Integrase Inhibitors chemical synthesis, HIV Integrase Inhibitors chemistry, Humans, Models, Molecular, Molecular Structure, Protein Binding drug effects, Structure-Activity Relationship, Tumor Cells, Cultured, para-Aminobenzoates chemical synthesis, para-Aminobenzoates chemistry, 1-Naphthylamine analogs & derivatives, Drug Discovery, HIV Integrase metabolism, HIV Integrase Inhibitors pharmacology, Intercellular Signaling Peptides and Proteins metabolism, para-Aminobenzoates pharmacology
Abstract

A series of N-aryl-naphthylamines, exemplified by the structures 11-16, were chosen for an in-house library screening to assay their ability to disrupt the interaction between the LEDGF cofactor and the HIV integrase. Structure modification led also to design and synthesize new compounds 17a-f. Compounds 11e,h,k,n, 13b, and 14 showed good activity in AlphaScreen assay. The most active compound 11e (IC50 = 2.5 μM) was selected for molecular modeling studies and showed a binding mode similar to the one of the known LEDGIN 8., (Copyright © 2015 Elsevier Masson SAS. All rights reserved.)

Published
2015
Full Text
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