The simulation shows amyloid-beta monomers nucleating and elongating into oligomers and fibrils, producing a sigmoidal aggregation-versus-time curve that shifts when you change monomer concentration or add a chaperone inhibitor.
Adjust the monomer concentration slider and toggle a chaperone molecule on or off to see the lag phase lengthen or shorten and the aggregation curve reshape in the live plot.
Monomer concentration slider and a chaperone/inhibitor toggle
The amyloid-beta 42 peptide has just two extra amino acids compared to the more common amyloid-beta 40 form, yet those two residues make it dramatically more prone to aggregating into plaques.
The simulation shows amyloid-beta monomers nucleating and elongating into oligomers and fibrils, producing a sigmoidal aggregation-versus-time curve that shifts when you change monomer concentration or add a chaperone inhibitor.
The simulation shows amyloid-beta monomers nucleating and elongating into oligomers and fibrils, producing a sigmoidal aggregation-versus-time curve that shifts when you change monomer concentration or add a chaperone inhibitor.
Adjust the monomer concentration slider and toggle a chaperone molecule on or off to see the lag phase lengthen or shorten and the aggregation curve reshape in the live plot.
The amyloid-beta 42 peptide has just two extra amino acids compared to the more common amyloid-beta 40 form, yet those two residues make it dramatically more prone to aggregating into plaques.