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SCIENTIFIC LITERATURE · MED

Identification of peptides interfering with the PP2Ac And LRRK2 interaction.

Biochim Biophys Acta Proteins Proteom · 2026-04-15

DOI: 10.1016/j.bbapap.2026.141145PMID: 41990985

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Research overview

The text below is the source article’s original abstract under a verified reuse license. cc by

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.

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