Self-Assembly of a Model Peptide Incorporating a Hexa-Histidine Sequence Attached to an Oligo-Alanine Sequence, and Binding to Gold NTA/Nickel Nanoparticles

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• 作者：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
• 刊名：Biomacromolecules
• 出版年：2014
• 出版时间：September 8, 2014
• 年：2014
• 卷：15
• 期：9
• 页码：3412-3420
• 全文大小：484K
• ISSN：1526-4602

文摘

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鈥檚), 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 尾-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.