Inhibition of

Leishmania infantum NADPH binding site X-ray crystal structure cluster docking procainamide derivatives procaine derivatives trypanothione reductase inhibition

Journal

Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009

Informations de publication

Date de publication:
01 Jan 2023
Historique:
received: 14 11 2022
revised: 15 12 2022
accepted: 28 12 2022
entrez: 8 1 2023
pubmed: 9 1 2023
medline: 11 1 2023
Statut: epublish

Résumé

As a result of the paucity of treatment, Leishmaniasis continues to provoke about 60,000 deaths every year worldwide. New molecules are needed, and drug discovery research is oriented toward targeting proteins crucial for parasite survival. Among them, trypanothione reductase (TR) is of remarkable interest owing to its vital role in We designed and synthesized new 3-amino-1-arylpropan-1-one derivatives structurally related to compound The newly synthesized compounds were screened at a concentration of 100 μM in in vitro assays and all of them proved to be active with residual activity percentages lower than 75%. Compounds

Sections du résumé

BACKGROUND BACKGROUND
As a result of the paucity of treatment, Leishmaniasis continues to provoke about 60,000 deaths every year worldwide. New molecules are needed, and drug discovery research is oriented toward targeting proteins crucial for parasite survival. Among them, trypanothione reductase (TR) is of remarkable interest owing to its vital role in
METHODS METHODS
We designed and synthesized new 3-amino-1-arylpropan-1-one derivatives structurally related to compound
RESULTS RESULTS
The newly synthesized compounds were screened at a concentration of 100 μM in in vitro assays and all of them proved to be active with residual activity percentages lower than 75%.
CONCLUSIONS CONCLUSIONS
Compounds

Identifiants

pubmed: 36615531
pii: molecules28010338
doi: 10.3390/molecules28010338
pmc: PMC9823735
pii:
doi:

Substances chimiques

trypanothione reductase EC 1.8.1.12
NADP 53-59-8
NADH, NADPH Oxidoreductases EC 1.6.-
Antiprotozoal Agents 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Sapienza University of Rome
ID : Ateneo 2019 (RM11916B6AFDBEBD)

Références

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Auteurs

Valentina Noemi Madia (VN)

Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Università di Roma, p.le Aldo Moro 5, 00185 Rome, Italy.

Davide Ialongo (D)

Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Università di Roma, p.le Aldo Moro 5, 00185 Rome, Italy.

Elisa Patacchini (E)

Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Università di Roma, p.le Aldo Moro 5, 00185 Rome, Italy.

Cécile Exertier (C)

Istituto di Biologia e Patologia Molecolari del CNR c/o Dipartimento di Scienze Biochimiche, Sapienza Università di Roma, p.le Aldo Moro 5, 00185 Roma, Italy.

Lorenzo Antonelli (L)

Istituto di Biologia e Patologia Molecolari del CNR c/o Dipartimento di Scienze Biochimiche, Sapienza Università di Roma, p.le Aldo Moro 5, 00185 Roma, Italy.
Dipartimento di Scienze Biochimiche, Sapienza Università di Roma, p.le Aldo Moro 5, 00185 Roma, Italy.

Gianni Colotti (G)

Istituto di Biologia e Patologia Molecolari del CNR c/o Dipartimento di Scienze Biochimiche, Sapienza Università di Roma, p.le Aldo Moro 5, 00185 Roma, Italy.

Antonella Messore (A)

Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Università di Roma, p.le Aldo Moro 5, 00185 Rome, Italy.

Valeria Tudino (V)

Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Università di Roma, p.le Aldo Moro 5, 00185 Rome, Italy.

Francesco Saccoliti (F)

D3 PharmaChemistry, Italian Institute of Technology, Via Morego 30, 16163 Genova, Italy.

Luigi Scipione (L)

Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Università di Roma, p.le Aldo Moro 5, 00185 Rome, Italy.

Andrea Ilari (A)

Istituto di Biologia e Patologia Molecolari del CNR c/o Dipartimento di Scienze Biochimiche, Sapienza Università di Roma, p.le Aldo Moro 5, 00185 Roma, Italy.

Roberta Costi (R)

Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Università di Roma, p.le Aldo Moro 5, 00185 Rome, Italy.

Roberto Di Santo (R)

Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Università di Roma, p.le Aldo Moro 5, 00185 Rome, Italy.

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Classifications MeSH