Amyloid fibrils are formed by a model surfactant-like peptide (Ala)(10)-(His)(6) containing a hexahistidine tag. This peptide undergoes a remarkable two-step self-assembly process with two distinct critical aggregation concentrations (cac's), probed by fluorescence techniques. A micromolar range cac is ascribed to the formation of prefibrillar structures, whereas a millimolar range cac is associated with the formation of well-defined but more compact fibrils. We examine the labeling of these model tagged amyloid fibrils using Ni-NTA functionalized gold nanoparticles (Nanogold). Successful labeling is demonstrated via electron microscopy imaging. The specificity of tagging does not disrupt the beta-sheet structure of the peptide fibrils. Binding of fibrils and Nanogold is found to influence the circular dichroism associated with the gold nanoparticle plasmon absorption band. These results highlight a new approach to the fabrication of functionalized amyloid fibrils and the creation of peptide/nanoparticle hybrid materials.

Self-assembly of a model peptide incorporating a hexa-histidine sequence attached to an Oligo-Alanine sequence, and binding to gold NTA/nickel nanoparticles / Hamley, I. W.; Kirkham, S.; Dehsorkhi, A.; Castelletto, V.; Adamcik, J.; Mezzenga, R.; Ruokolainen, J.; Mazzuca, C.; Gatto, E.; Venanzi, M.; Placidi, E.; Bilalis, P.; Iatrou, H.. - In: BIOMACROMOLECULES. - ISSN 1525-7797. - 15:9(2014), pp. 3412-3420. [10.1021/bm500950c]

Self-assembly of a model peptide incorporating a hexa-histidine sequence attached to an Oligo-Alanine sequence, and binding to gold NTA/nickel nanoparticles

Placidi E.;
2014

Abstract

Amyloid fibrils are formed by a model surfactant-like peptide (Ala)(10)-(His)(6) containing a hexahistidine tag. This peptide undergoes a remarkable two-step self-assembly process with two distinct critical aggregation concentrations (cac's), probed by fluorescence techniques. A micromolar range cac is ascribed to the formation of prefibrillar structures, whereas a millimolar range cac is associated with the formation of well-defined but more compact fibrils. We examine the labeling of these model tagged amyloid fibrils using Ni-NTA functionalized gold nanoparticles (Nanogold). Successful labeling is demonstrated via electron microscopy imaging. The specificity of tagging does not disrupt the beta-sheet structure of the peptide fibrils. Binding of fibrils and Nanogold is found to influence the circular dichroism associated with the gold nanoparticle plasmon absorption band. These results highlight a new approach to the fabrication of functionalized amyloid fibrils and the creation of peptide/nanoparticle hybrid materials.
2014
Gold; Histidine; Metal Nanoparticles; Nickel; Peptides
01 Pubblicazione su rivista::01a Articolo in rivista
Self-assembly of a model peptide incorporating a hexa-histidine sequence attached to an Oligo-Alanine sequence, and binding to gold NTA/nickel nanoparticles / Hamley, I. W.; Kirkham, S.; Dehsorkhi, A.; Castelletto, V.; Adamcik, J.; Mezzenga, R.; Ruokolainen, J.; Mazzuca, C.; Gatto, E.; Venanzi, M.; Placidi, E.; Bilalis, P.; Iatrou, H.. - In: BIOMACROMOLECULES. - ISSN 1525-7797. - 15:9(2014), pp. 3412-3420. [10.1021/bm500950c]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1326629
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