The influence of cations on α-lactalbumin amyloid aggregation

There is limited knowledge regarding α-lactalbumin amyloid aggregation and its mechanism. We examined the formation of α-lactalbumin amyloid fibrils (α-LAF) in the presence of cations (Mg 2+ , Ca 2+ , Na + , K + , NH 4 + , and Cs + ) in the form of chloride salts at two concentrations. We have shown that studied cations affect the conformation of α-lactalbumin, the kinetics of its amyloid formation, morphology, and secondary structure of α-LAF in a different manner. The higher salts concentration significantly accelerated the aggregation process. Both salt concentrations stabilized α-lactalbumin's secondary structure. However, the presence of divalent cations resulted in shorter fibrils with less β-sheet content. Moreover, strongly hydrated Mg 2+ significantly altered α-lactalbumin's tertiary structure, followed by Na + , NH 4 + , K + , and weakly hydrated Cs + . On the other hand, Ca 2+ , despite being also strongly hydrated, stabilized the tertiary structure, supposedly due to its high affinity towards α-lactalbumin. Yet, Ca 2+ was not able to inhibit α-lactalbumin amyloid aggregation. Graphic abstract