TY - JOUR
TI - Self-Assembly of a Model Peptide Incorporating a Hexa-Histidine Sequence Attached to an Oligo-Alanine Sequence, and Binding to Gold NTA/Nickel Nanoparticles
AU - Ian W. Hamley
AU - Steven Kirkham
AU - Ashkan Dehsorkhi
AU - Valeria Castelletto
AU - Jozef Adamcik
AU - Raffaele Mezzenga
AU - Janne Ruokolainen
AU - Claudia Mazzuca
AU - Emanuela Gatto
AU - Mariano Venanzi
AU - Ernesto Placidi
AU - Panayiotis Bilalis
AU - Hermis Iatrou
JO - Biomacromolecules
PY - 2014
VL - 15
TODO - 9
SP - 3412--3420
PB - American Chemical Society (ACS)
SN - 1525-7797, 1526-4602
TODO - 10.1021/bm500950c
TODO - 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
TODO - 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.
ER -