Journal
EUROPEAN JOURNAL OF PHARMACEUTICAL SCIENCES
Volume 154, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.ejps.2020.105510
Keywords
Peptidomimetics; OGT; Inhibitors; Molecular dynamics; O-GlcNAc; Glycosylation; Post-translational modification; Molecular docking; Molecular modeling
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Funding
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior-Brazil (CAPES)
- National Council for Scientific and Technological Development (Conselho Nacional de Desenvolvimento Cientifico e Tecnologico - CNPq)
- Carlos Chagas Filho Foundation for Support of Research of the State of Rio de Janeiro (Fundacao Carlos Chagas Filho de Amparo a Pesquisa do Estado do Rio de Janeiro - FAPERJ)
- Cancer Foundation (Fundacao do Cancer)
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The vital enzyme O-linked beta-N-acetylglucosamine transferase (OGT) catalyzes the O-GlcNAcylation of intracellular proteins coupling the metabolic status to cellular signaling and transcription pathways. Aberrant levels of O-GlcNAc and OGT have been linked to metabolic diseases as cancer and diabetes. Here, a new series of peptidomimetic OGT inhibitors was identified highlighting the compound LQMed 330, which presented better IC50 compared to the most potent inhibitors found in the literature. Molecular modeling study of selected inhibitors into the OGT binding site provided insight into the behavior by which these compounds interact with the enzyme. The results obtained in this study provided new perspectives on the design and synthesis of highly specific OGT inhibitors.
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