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Py-CoMFA, docking, and molecular dynamics simulations of Leishmania (L.) amazonensis arginase inhibitors.
Camargo, Priscila Goes; Dos Santos, Carine Ribeiro; Girão Albuquerque, Magaly; Rangel Rodrigues, Carlos; Lima, Camilo Henrique da Silva.
Afiliación
  • Camargo PG; Faculdade de Farmácia, Departamento de Fármacos e Medicamentos, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
  • Dos Santos CR; Laboratório de Modelagem Molecular (LabMMol), Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
  • Girão Albuquerque M; Laboratório de Modelagem Molecular (LabMMol), Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
  • Rangel Rodrigues C; Faculdade de Farmácia, Departamento de Fármacos e Medicamentos, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil. rangelfarmacia@gmail.com.
  • Lima CHDS; Laboratório de Modelagem Molecular (LabMMol), Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil. camilolima@iq.ufrj.br.
Sci Rep ; 14(1): 11575, 2024 05 21.
Article en En | MEDLINE | ID: mdl-38773273
ABSTRACT
Leishmaniasis is a disease caused by a protozoan of the genus Leishmania, affecting millions of people, mainly in tropical countries, due to poor social conditions and low economic development. First-line chemotherapeutic agents involve highly toxic pentavalent antimonials, while treatment failure is mainly due to the emergence of drug-resistant strains. Leishmania arginase (ARG) enzyme is vital in pathogenicity and contributes to a higher infection rate, thus representing a potential drug target. This study helps in designing ARG inhibitors for the treatment of leishmaniasis. Py-CoMFA (3D-QSAR) models were constructed using 34 inhibitors from different chemical classes against ARG from L. (L.) amazonensis (LaARG). The 3D-QSAR predictions showed an excellent correlation between experimental and calculated pIC50 values. The molecular docking study identified the favorable hydrophobicity contribution of phenyl and cyclohexyl groups as substituents in the enzyme allosteric site. Molecular dynamics simulations of selected protein-ligand complexes were conducted to understand derivatives' interaction modes and affinity in both active and allosteric sites. Two cinnamide compounds, 7g and 7k, were identified, with similar structures to the reference 4h allosteric site inhibitor. These compounds can guide the development of more effective arginase inhibitors as potential antileishmanial drugs.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arginasa / Inhibidores Enzimáticos / Simulación de Dinámica Molecular / Simulación del Acoplamiento Molecular / Leishmania Idioma: En Revista: Sci Rep Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arginasa / Inhibidores Enzimáticos / Simulación de Dinámica Molecular / Simulación del Acoplamiento Molecular / Leishmania Idioma: En Revista: Sci Rep Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido