Nucleation of Amyloid Oligomers by RepA-WH1-Prionoid-Functionalized Gold Nanorods
Dr. Cristina Fernández
Department of Cellular and Molecular Biology, Centro de Investigaciones Biológicas—CSIC, 28040 Madrid, Spain
These authors contributed equally to this work.
Search for more papers by this authorGuillermo González-Rubio
Departamento de Química Física I, Universidad Complutense de Madrid, Avda. Complutense s/n, 28040 Madrid, Spain
BioNanoPlasmonics Laboratory, CIC biomaGUNE, Donostia—, 20009 San Sebastián, Spain
These authors contributed equally to this work.
Search for more papers by this authorDr. Judith Langer
BioNanoPlasmonics Laboratory, CIC biomaGUNE, Donostia—, 20009 San Sebastián, Spain
Search for more papers by this authorProf. Gloria Tardajos
Departamento de Química Física I, Universidad Complutense de Madrid, Avda. Complutense s/n, 28040 Madrid, Spain
Search for more papers by this authorProf. Luis M. Liz-Marzán
BioNanoPlasmonics Laboratory, CIC biomaGUNE, Donostia—, 20009 San Sebastián, Spain
Ikerbasque, Basque Foundation for Science, 48013 Bilbao, Spain
Biomedical Research Networking Center in Bioengineering, Biomaterials, and Nanomedicine, CIBER-BBN, Spain
Search for more papers by this authorCorresponding Author
Prof. Rafael Giraldo
Department of Cellular and Molecular Biology, Centro de Investigaciones Biológicas—CSIC, 28040 Madrid, Spain
Search for more papers by this authorCorresponding Author
Dr. Andrés Guerrero-Martínez
Departamento de Química Física I, Universidad Complutense de Madrid, Avda. Complutense s/n, 28040 Madrid, Spain
Search for more papers by this authorDr. Cristina Fernández
Department of Cellular and Molecular Biology, Centro de Investigaciones Biológicas—CSIC, 28040 Madrid, Spain
These authors contributed equally to this work.
Search for more papers by this authorGuillermo González-Rubio
Departamento de Química Física I, Universidad Complutense de Madrid, Avda. Complutense s/n, 28040 Madrid, Spain
BioNanoPlasmonics Laboratory, CIC biomaGUNE, Donostia—, 20009 San Sebastián, Spain
These authors contributed equally to this work.
Search for more papers by this authorDr. Judith Langer
BioNanoPlasmonics Laboratory, CIC biomaGUNE, Donostia—, 20009 San Sebastián, Spain
Search for more papers by this authorProf. Gloria Tardajos
Departamento de Química Física I, Universidad Complutense de Madrid, Avda. Complutense s/n, 28040 Madrid, Spain
Search for more papers by this authorProf. Luis M. Liz-Marzán
BioNanoPlasmonics Laboratory, CIC biomaGUNE, Donostia—, 20009 San Sebastián, Spain
Ikerbasque, Basque Foundation for Science, 48013 Bilbao, Spain
Biomedical Research Networking Center in Bioengineering, Biomaterials, and Nanomedicine, CIBER-BBN, Spain
Search for more papers by this authorCorresponding Author
Prof. Rafael Giraldo
Department of Cellular and Molecular Biology, Centro de Investigaciones Biológicas—CSIC, 28040 Madrid, Spain
Search for more papers by this authorCorresponding Author
Dr. Andrés Guerrero-Martínez
Departamento de Química Física I, Universidad Complutense de Madrid, Avda. Complutense s/n, 28040 Madrid, Spain
Search for more papers by this authorAbstract
Understanding protein amyloidogenesis is an important topic in protein science, fueled by the role of amyloid aggregates, especially oligomers, in the etiology of a number of devastating human degenerative diseases. However, the mechanisms that determine the formation of amyloid oligomers remain elusive due to the high complexity of the amyloidogenesis process. For instance, gold nanoparticles promote or inhibit amyloid fibrillation. We have functionalized gold nanorods with a metal-chelating group to selectively immobilize soluble RepA-WH1, a model synthetic bacterial prionoid, using a hexa-histidine tag (H6). H6-RepA-WH1 undergoes stable amyloid oligomerization in the presence of catalytic concentrations of anisotropic nanoparticles. Then, in a physically separated event, such oligomers promote the growth of amyloid fibers of untagged RepA-WH1. SERS spectral changes of H6-RepA-WH1 on spherical citrate-AuNP substrates provide evidence for structural modifications in the protein, which are compatible with a gradual increase in β-sheet structure, as expected in amyloid oligomerization.
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