Amyloid fibrils are formed by soluble proteins that, through protein unfolding, assemble into non-degradable insoluble β-sheet fibers. These aggregates cause many Amyloidosis diseases by bonding in different body organs and becoming obstructive in several biological processes. A recent study conducted by the University of Puerto Rico in Mayagüez revealed that hydrogen sulfide (H2S) inhibits amyloid formation. More so, as the concentration of H2S increases in the samples, AFM imaging shows a change in protein morphology from fibrils to overlapping spherules that conserve the native protein’s secondary structure (Figure 1). The morphology of samples with H2S resembles those of the oligomers present in the nucleation process during the amyloid fibril formation curve's lag phase. This protein modification or oligomer aggregation generates an alternative energetic pathway that leads to stabilized spherulites and fibrils' inhibition. We intend to determine the difference in stability between the fibrils and the newly formed non-cytotoxic spherulites.

Determination of H2S induced spherulite structures in amyloid formation

ACS Spring Meeting 2021

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