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HSP10 also demonstrates independent roles in binding to misfolded proteins and interacts with several amyloidogenic client proteins. Using a variety of biophysical and biochemical methods, we studied the interactions of HSP10 with the amyloidogenic protein \u03b1\u2010synuclein (\u03b1\u2010syn) associated with Parkinson's disease. HSP10 efficiently inhibited fibril formation of wild type (WT) and disease\u2010mutant A30P \u03b1\u2010syn at sufficient concentrations of chaperone by both binding to \u03b1\u2010syn monomers and by blocking secondary nucleation on fibril surfaces. However, under sub\u2010stoichiometric conditions, below 1:5 (HSP10:\u03b1\u2010syn), the chaperone sequestered multiple A30P \u03b1\u2010syn monomers and thereby promoted nucleation of fibril formation with a magnitude comparable to the efficacy of seeding with preformed fibrils. 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