Part I: Applying The Boger A-Helix Mimetic Motif to Potentially Modulate Beclin-1 Mediated Protein-Protein Interactions Relating to Autophagic Flux for Oncological Purposes. Part II: Utilizing Peptidomimetics to Target The 5-HT2CR Through its Interaction with the Protein and Tumor Suppressor Phosphatase and Tensin Homologue (PTEN).



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Beclin-1 is a protein required for autophagosome formation; thus, it is an essential protein regarding macroautophagy. The Kritzer group previously designed the DD5-o peptide to induce autophagy. The DD5-o peptide shows a helical structure in solution. In the last 20 years, there has been a lot of synthetic progress in developing non-peptide α-helix mimetics. We applied the Boger α-helix mimic to target one-helical-face of the protein Beclin-1 for potential modulation of autophagic flux for prospective use in oncology. We have synthesized a variety of compounds, and they have been sent to our collaborators for biological assays to be performed. The serotonin 2C receptor has been implicated in a variety of psychiatric disorders. Previously, a peptidomimetic was found to disrupt the association between the serotonin 2C receptor and the Phosphatase and Tensin Homologue (PTEN). This disruption enhances serotonin 2C receptor downstream signaling and potentiates serotonin 2C receptor agonists. We synthesized a variety of analogues of the peptidomimetic, and these analogues have been sent to our collaborators for biological assays to be performed. We also attempted new synthetic routes to the bioactive peptidomimetic.



Beclin-1, helical, α-helix, α-helix mimics, α-helix mimetics, one-helical-face, serotonin 2C receptor, Phosphatase and Tensin Homologue, PTEN, peptidomimetic, β-Proline, (S)-β-Proline, (R)-β-Proline