(627d) Amyloid Aggregation of Bacillus Circulans Xylanase Under Native Conditions and Its Modulation By ?-Amyloid-Derived Peptide Fragments
AIChE Annual Meeting
Thursday, November 14, 2019 - 8:54am to 9:12am
In this research, we studied the amyloid aggregation of a globular protein, Bacillus circulans xylanase (BCX)âan endoâÎ²â1-4âxylanase catalyzing the hydrolysis of the polysaccharide xylanâupon fusion or addition of nonâselfâaggregating fragments, KLVFWAK and ELVFWAE, which were derived from the key amyloidogenic domain of Î²-amyloid (AÎ²). To the best of our knowledge, this is the first time that the wildâtype BCX has been shown to form amyloid fibrils under native conditions. Our results also support the view that the kinetic stability of BCX is closely related to its amyloid aggregation. Moreover, our study demonstrates that the impacts of the nonâselfâaggregating AÎ²âderived fragments on BCX amyloid aggregation might vary depending on whether the fragments were fused to or simply mixed with BCX. Collectively, this study 1) provides insight into a globular protein's amyloid aggregation under native conditions, its kinetic stability, and the modulation thereof by AÎ²âderived, nonâselfâaggregating fragments and 2) demonstrates that these fragments are useful for modulating amyloid aggregation for some, though not all, proteins.