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Development of a novel catalytic amyloid displaying a metal-dependent ATPase-like activity

Monasterio, Octavio ; Nova, Esteban ; Diaz-Espinoza, Rodrigo

Biochemical and biophysical research communications, 2017-01, Vol.482 (4), p.1194-1200 [Periódico revisado por pares]

United States: Elsevier Inc

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Development of a novel catalytic amyloid displaying a metal-dependent ATPase-like activity
Autor: Monasterio, Octavio ; Nova, Esteban ; Diaz-Espinoza, Rodrigo
Assuntos: Adenosine Diphosphate - chemistry ; Adenosine Monophosphate - chemistry ; Adenosine Triphosphatases - chemistry ; Adenosine Triphosphate - chemistry ; Amyloid ; Amyloid - chemistry ; Amyloidogenic Proteins ; ATP ; Catalysis ; Catalytic Domain ; Computer Simulation ; Humans ; Hydrogen-Ion Concentration ; Hydrolysis ; Ions ; Magnesium - chemistry ; Manganese ; Manganese - chemistry ; Metals - chemistry ; Peptide ; Peptides - chemistry ; Thiazoles - chemistry
É parte de: Biochemical and biophysical research communications, 2017-01, Vol.482 (4), p.1194-1200
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SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: Amyloids are protein aggregates of highly regular structure that are involved in diverse pathologies such as Alzheimer's and Parkinson's disease. Recent evidence has shown that under certain conditions, small peptides can self-assemble into amyloids that exhibit catalytic reactivity towards certain compounds. Here we report a novel peptide with a sequence derived from the active site of RNA polymerase that displays hydrolytic activity towards ATP. The catalytic reaction proceeds in the presence of the divalent metal manganese and the products are ADP and AMP. The kinetic data shows a substrate-dependent saturation of the activity with a maximum rate achieved at around 1 mM ATP. At higher ATP concentrations, we also observed substrate inhibition of the activity. The self-assembly of the peptide into amyloids is strictly metal-dependent and required for the catalysis. Our results show that aspartate-containing amyloids can also be catalysts under conditions that include interactions with metals. Moreover, we show for the first time an amyloid that exerts reactivity towards a biologically essential molecule. •A small peptide aggregates into amyloids in a metal-dependent manner at pH 8.0•The peptide catalyzes the hydrolysis of ATP into ADP and AMP using manganese.•Amyloid formation is required for the activity.•Metal-interacting acidic residues can be catalytic in the amyloid conformation.•Biologically relevant molecules can be target for reactive amyloids.
Editor: United States: Elsevier Inc
Idioma: Inglês

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Development of a novel catalytic amyloid displaying a metal-dependent ATPase-like activity

Monasterio, Octavio ; Nova, Esteban ; Diaz-Espinoza, Rodrigo

United States: Elsevier Inc

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