Identification of peptides interfering with the PP2Ac And LRRK2 interaction.
Identification of peptides interfering with the PP2Ac And LRRK2 interaction.
Where did the research take place?
The study site has not been established. Author addresses may differ from where the research occurred.
Paris, FR · Author affiliation
Unité de Technologies Chimiques et Biologiques pour la Santé, INSERM U1267 - CNRS UMR8258, Université Paris Cité, Faculté de Pharmacie, France. Electronic address: angelita.rebollo@parisdescartes.fr.Location evidence
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Original abstract
Using the PEP-scan approach, we have identified the binding site of PP2Ac to LRRK2, a protein associated with Parkinson's disease. We also have identified the binding site of LRRK2 to PP2Ac, referred to as mirror peptide. All isolated fragments are predicted to be solvent-accessible and are compatible with contributing to LRRK2/PP2Ac interaction except for peptide M2. The In vitro competition experiment demonstrated that peptide P3 and M1 effectively compete PP2A/LRRK2 interaction. Both appear to have propensity to adopt helical conformation. These newly generated peptides can be tools to investigate the role of PP2A/LRRK2 interaction under both physiological and pathological conditions.