Many proteins can aggregate into amyloid fibrils. Fibril elongation has many sim

Question

Many proteins can aggregate into amyloid fibrils. Fibril elongation has many similarities to an enzymatic reaction. Experimental data on insulin amyloid-like fibril elongation suggest that the formation of fibrils follows Michaelis-Menten kinetics as shown in the below figure.

Sonication is commonly used to create amyloid fibril. Suggest a hypothesis as to how sonication facilitates conversion.

journal.pone.0068684.g002

Explanation / Answer

The amyloid fibrils are fibrils made up of monomeric units and amyloid fibrillation can be considered similar to crystallization which occurs only in a super-saturated solution where the concentration of monomer units is above a certain critical concentration level. It primarily comprises of nucleation and growth processes.

Ultrasonication has been known to induce spontaneous fibrillation in amyloid proteins. The hypothysed mechanism suggests that when cavitation develops as a result of sonication waves generated in the solution, they lead to generation of hydrophobic surfaces. Interaction with these surfaces leads to aggregation of the monomers leading to fibrillation. This occurs only at concentrations at Mtot level.

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