Parkinson's Disease (PD) is associated with the neuronal accumulation b sheet rich form of the protein a synuclein (aSyn) into aggregates called Lewy Bodies (LBs). A connection between PD and the 14-3-3 chaperone like protein family was recently proposed, being that several 14-3-3 isoforms can interact with aSyn and are found in LBs.In vitro aSyn aggregation kinetics in the presence of 14-3-3h, followed by fluorescence polarization spectroscopy, showed that 14-3-3h inhibits the formation of aSyn fibrils. NMR, TEM and AFM experiments demonstrated that 14-3-3h does not interact with monomeric aSyn and is not able to disaggregate amyloid fibrils; instead, it interacts with oligomeric aSyn aggregation intermediates leading to an alternative amyloidogenic pathway yielding products that are morphologically different from canonical aSyn fibrils. 14-3-3h was also found to interfere with the accretion of aSyn monomers on preformed fibrillar seeds, with drastically different effects based on the type of seed used. Finally, starting from seeds, 14-3-3h is sequestered within aSyn fibrils as demonstrated by immunogold TEM assay. A HEK293 cell line was tested for the inhibition of aSyn aggregation and rescue by 14-3-3 in a confocal fluorescence microscopy assay, where aggregation was triggered by fibrillar seeds. The cellular results confirmed the observations made in vitro.