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Symmetric molecules with 1,4-triazole moieties as potent inhibitors of tumour-associated lactate dehydrogenase-A.
Altamimi, Abdul-Malek S; Alafeefy, Ahmed M; Balode, Agnese; Vozny, Igor; Pustenko, Aleksandrs; El Shikh, Mohey Eldin; Alasmary, Fatmah A S; Abdel-Gawad, Sherif A; Zalubovskis, Raivis.
Afiliação
  • Altamimi AS; a Department of Pharmaceutical Chemistry, College of Pharmacy , Prince Sattam Bin Abdulaziz University , Alkharj , Saudi Arabia.
  • Alafeefy AM; b Department of Chemistry , Kulliyyah of Science, International Islamic University Malaysia.
  • Balode A; c Latvian Institute of Organic Synthesis , Riga , Latvia.
  • Vozny I; d Institute of Technology of Organic Chemistry, Faculty of Materials Science and Applied Chemistry , Riga Technical University , Riga , Latvia.
  • Pustenko A; c Latvian Institute of Organic Synthesis , Riga , Latvia.
  • El Shikh ME; c Latvian Institute of Organic Synthesis , Riga , Latvia.
  • Alasmary FAS; d Institute of Technology of Organic Chemistry, Faculty of Materials Science and Applied Chemistry , Riga Technical University , Riga , Latvia.
  • Abdel-Gawad SA; e Experimental Medicine and Rheumatology , William Harvey Research Institute, Queen Mary University of London , London , UK.
  • Zalubovskis R; f Chemistry Department, College of Science , King Saud University , Saudi Arabia , Riyadh.
J Enzyme Inhib Med Chem ; 33(1): 147-150, 2018 Dec.
Article em En | MEDLINE | ID: mdl-29199484
A series of symmetric molecules incorporating aryl or pyridyl moieties as central core and 1,4-substituted triazoles as a side bridge was synthesised. The new compounds were investigated as lactate dehydro-genase (LDH, EC 1.1.1.27) inhibitors. The cancer associated LDHA isoform was inhibited with IC50 = 117-174 µM. Seven compounds exhibited better LDHA inhibition (IC50 117-136 µM) compared to known LDH inhibitor - galloflavin (IC50 157 µM).
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Triazóis / Inibidores Enzimáticos / Isocumarinas / L-Lactato Desidrogenase Tipo de estudo: Risk_factors_studies Limite: Humans Idioma: En Revista: J Enzyme Inhib Med Chem Assunto da revista: BIOQUIMICA / QUIMICA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Arábia Saudita País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Triazóis / Inibidores Enzimáticos / Isocumarinas / L-Lactato Desidrogenase Tipo de estudo: Risk_factors_studies Limite: Humans Idioma: En Revista: J Enzyme Inhib Med Chem Assunto da revista: BIOQUIMICA / QUIMICA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Arábia Saudita País de publicação: Reino Unido