@article{2959200,
    title = "Self-Assembly of a Model Peptide Incorporating a Hexa-Histidine Sequence Attached to an Oligo-Alanine Sequence, and Binding to Gold NTA/Nickel Nanoparticles",
    author = "Ian W. Hamley and Steven Kirkham and Ashkan Dehsorkhi and Valeria Castelletto and Jozef Adamcik and Raffaele Mezzenga and Janne Ruokolainen and Claudia Mazzuca and Emanuela Gatto and Mariano Venanzi and Ernesto Placidi and Panayiotis Bilalis and Hermis Iatrou",
    journal = "Biomacromolecules",
    year = "2014",
    volume = "15",
    number = "9",
    pages = "3412--3420",
    publisher = "American Chemical Society (ACS)",
    issn = "1525-7797, 1526-4602",
    doi = "10.1021/bm500950c",
    keywords = "Amino acids;  Dichroism;  Glycoproteins;  Gold;  Hybrid materials;  Metal nanoparticles;  Self assembly, Critical aggregation concentration;  Fluorescence technique;  Functionalized gold nanoparticles;  Gold Nanoparticles;  Millimolar range;  Plasmon absorption bands;  Self assembly process;  Surfactant-like peptides, Peptides, alanine;  amyloid;  gold nanoparticle;  hexahistidine;  metal nanoparticle;  nickel nanoparticle;  nitrilotriacetic acid;  peptide;  unclassified drug;  gold;  histidine;  metal nanoparticle;  nickel;  peptide;  polyalanine;  polyhistidine, amino acid sequence;  Article;  circular dichroism;  hybrid;  labeling index;  nanofabrication;  particle size;  peptide synthesis;  protein assembly;  surface plasmon resonance;  transmission electron microscopy, Gold;  Histidine;  Metal Nanoparticles;  Nickel;  Peptides",
    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. © 2014 American Chemical Society."
}