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

Ian W. Hamley*, Steven Kirkham, Ashkan Dehsorkhi, Valeria Castelletto, Jozef Adamcik, Raffaele Mezzenga, Janne Ruokolainen, Claudia Mazzuca, Emanuela Gatto, Mariano Venanzi, Ernesto Placidi, Panayiotis Bilalis, Hermis Iatrou

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Amyloid fibrils are formed by a model surfactant-like peptide (Ala)10-(His)6 containing a hexa-histidine 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 β-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.

Original languageEnglish (US)
Pages (from-to)3412-3420
Number of pages9
JournalBiomacromolecules
Volume15
Issue number9
DOIs
StatePublished - Sep 8 2014

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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