Functional characterization of the ATPase-like activity displayed by a catalytic amyloid

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Functional characterization of the ATPase-like activity displayed by a catalytic amyloid. / castillo-Caceres, Claudio; Duran-Meza, Eva; Nova, Esteban; Araya Secchi, Raul Rene; Monasterio, Octavio; Diaz-Espinoza, Rodrigo.

I: B B A - General Subjects, Bind 1865, Nr. 1, 129729, 2021.

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Harvard

castillo-Caceres, C, Duran-Meza, E, Nova, E, Araya Secchi, RR, Monasterio, O & Diaz-Espinoza, R 2021, 'Functional characterization of the ATPase-like activity displayed by a catalytic amyloid', B B A - General Subjects, bind 1865, nr. 1, 129729. https://doi.org/10.1016/j.bbagen.2020.129729

APA

castillo-Caceres, C., Duran-Meza, E., Nova, E., Araya Secchi, R. R., Monasterio, O., & Diaz-Espinoza, R. (2021). Functional characterization of the ATPase-like activity displayed by a catalytic amyloid. B B A - General Subjects, 1865(1), [129729]. https://doi.org/10.1016/j.bbagen.2020.129729

Vancouver

castillo-Caceres C, Duran-Meza E, Nova E, Araya Secchi RR, Monasterio O, Diaz-Espinoza R. Functional characterization of the ATPase-like activity displayed by a catalytic amyloid. B B A - General Subjects. 2021;1865(1). 129729. https://doi.org/10.1016/j.bbagen.2020.129729

Author

castillo-Caceres, Claudio ; Duran-Meza, Eva ; Nova, Esteban ; Araya Secchi, Raul Rene ; Monasterio, Octavio ; Diaz-Espinoza, Rodrigo. / Functional characterization of the ATPase-like activity displayed by a catalytic amyloid. I: B B A - General Subjects. 2021 ; Bind 1865, Nr. 1.

Bibtex

@article{65d6a253972a456b9fc49ed11e88e0a3,
title = "Functional characterization of the ATPase-like activity displayed by a catalytic amyloid",
abstract = "Background: Amyloids are highly ordered polypeptide aggregates stabilized by a beta-sheet structural core. Though classically associated to pathology, reports on novel functional roles of these proteins have increasingly emerged in the past decade. Moreover, the recent discovery that amyloids formed with rationally designed small peptides can exhibit catalytic reactivity has opened up new opportunities in both biology and biotechnology. The observed activities typically require the binding of divalent metals, giving rise to active metal-amyloid complexes. Methods: Peptide (SDIDVFI) was aggregated in vitro. The structure of the self-assembled species was analyzed using fluorescence, transmission electron microscopy, circular dichroism and computational modeling. A kinetic characterization of the emerging catalytic activity was performed. Results: The peptide self-assembled into canonical amyloids that exhibited catalytic activity towards hydrolysis of the phosphoanhydride bonds of adenosine triphosphate (ATP), partially mimicking an ATPase-like enzyme. Both amyloid formation and activity are shown to depend on manganese (Mn2+) binding. The activity was not restricted to ATP but also affected all other ribonucleotides (GTP, CTP and UTP). Peptides carrying a single aspartate exhibited a similar activity. Conclusions: The phosphoanhydride bonds appear as the main specificity target of the Mn2+-amyloid complex. A single aspartate per peptide is sufficient to enable the hydrolytic activity. General significance: Catalytic amyloids are shown for the first time to catalyze the hydrolysis of all four ribonucleotides. Our results should contribute towards understanding the biological implications of amyloidmediated reactivity as well as in the design of future catalytic amyloids for biotechnological applications.",
author = "Claudio castillo-Caceres and Eva Duran-Meza and Esteban Nova and {Araya Secchi}, {Raul Rene} and Octavio Monasterio and Rodrigo Diaz-Espinoza",
year = "2021",
doi = "10.1016/j.bbagen.2020.129729",
language = "English",
volume = "1865",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Functional characterization of the ATPase-like activity displayed by a catalytic amyloid

AU - castillo-Caceres, Claudio

AU - Duran-Meza, Eva

AU - Nova, Esteban

AU - Araya Secchi, Raul Rene

AU - Monasterio, Octavio

AU - Diaz-Espinoza, Rodrigo

PY - 2021

Y1 - 2021

N2 - Background: Amyloids are highly ordered polypeptide aggregates stabilized by a beta-sheet structural core. Though classically associated to pathology, reports on novel functional roles of these proteins have increasingly emerged in the past decade. Moreover, the recent discovery that amyloids formed with rationally designed small peptides can exhibit catalytic reactivity has opened up new opportunities in both biology and biotechnology. The observed activities typically require the binding of divalent metals, giving rise to active metal-amyloid complexes. Methods: Peptide (SDIDVFI) was aggregated in vitro. The structure of the self-assembled species was analyzed using fluorescence, transmission electron microscopy, circular dichroism and computational modeling. A kinetic characterization of the emerging catalytic activity was performed. Results: The peptide self-assembled into canonical amyloids that exhibited catalytic activity towards hydrolysis of the phosphoanhydride bonds of adenosine triphosphate (ATP), partially mimicking an ATPase-like enzyme. Both amyloid formation and activity are shown to depend on manganese (Mn2+) binding. The activity was not restricted to ATP but also affected all other ribonucleotides (GTP, CTP and UTP). Peptides carrying a single aspartate exhibited a similar activity. Conclusions: The phosphoanhydride bonds appear as the main specificity target of the Mn2+-amyloid complex. A single aspartate per peptide is sufficient to enable the hydrolytic activity. General significance: Catalytic amyloids are shown for the first time to catalyze the hydrolysis of all four ribonucleotides. Our results should contribute towards understanding the biological implications of amyloidmediated reactivity as well as in the design of future catalytic amyloids for biotechnological applications.

AB - Background: Amyloids are highly ordered polypeptide aggregates stabilized by a beta-sheet structural core. Though classically associated to pathology, reports on novel functional roles of these proteins have increasingly emerged in the past decade. Moreover, the recent discovery that amyloids formed with rationally designed small peptides can exhibit catalytic reactivity has opened up new opportunities in both biology and biotechnology. The observed activities typically require the binding of divalent metals, giving rise to active metal-amyloid complexes. Methods: Peptide (SDIDVFI) was aggregated in vitro. The structure of the self-assembled species was analyzed using fluorescence, transmission electron microscopy, circular dichroism and computational modeling. A kinetic characterization of the emerging catalytic activity was performed. Results: The peptide self-assembled into canonical amyloids that exhibited catalytic activity towards hydrolysis of the phosphoanhydride bonds of adenosine triphosphate (ATP), partially mimicking an ATPase-like enzyme. Both amyloid formation and activity are shown to depend on manganese (Mn2+) binding. The activity was not restricted to ATP but also affected all other ribonucleotides (GTP, CTP and UTP). Peptides carrying a single aspartate exhibited a similar activity. Conclusions: The phosphoanhydride bonds appear as the main specificity target of the Mn2+-amyloid complex. A single aspartate per peptide is sufficient to enable the hydrolytic activity. General significance: Catalytic amyloids are shown for the first time to catalyze the hydrolysis of all four ribonucleotides. Our results should contribute towards understanding the biological implications of amyloidmediated reactivity as well as in the design of future catalytic amyloids for biotechnological applications.

U2 - 10.1016/j.bbagen.2020.129729

DO - 10.1016/j.bbagen.2020.129729

M3 - Journal article

C2 - 32916204

VL - 1865

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 1

M1 - 129729

ER -

ID: 248602889