Abstract
Aβ1–40 coated 20 nm gold colloidal nanoparticles exhibit a reversible color change as pH is externally altered between pH 4 and 10. This reversible process may contain important information on the initial reversible step reported for the fibrillogenesis of Aβ (a hallmark of Alzheimer’s disease). We examined this reversible color change by microscopic investigations. AFM images on graphite surfaces revealed the morphology of Aβ aggregates with gold colloids. TEM images clearly demonstrate the correspondence between spectroscopic features and conformational changes of the gold colloid.
Highlights
Nanoscale materials have revolutionalized the function and use of materials in many fields including the biomedical field
528 + 1 nm can be regarded as the free gold colloidal band and more free gold colloidal nanoparticle surfaces are produced as the pH changes are repeated
The Transmission Electron Microscopy (TEM) images were collected for 20 nm gold colloid alone, 20 nm gold colloid coated ovalbumin, and 20 nm gold colloid coated with A 1-40 that were cycled between pH 4 and pH 10
Summary
Nanoscale materials have revolutionalized the function and use of materials in many fields including the biomedical field. Until now, limited studies have been performed to investigate this phenomenon due to the theoretical [4547] and experimental [48-54] complexity of secondary and tertiary protein structures forming from non-native conformations at an interface This is a key step of fibrillogenesis, yet most in vitro studies overlook this step and focus on the aggregation of A prepared in solution. This conformation of the A self assembly on the membrane surface may be seen when A conjugates on the surface of gold colloidal nanoparticle. This reversibility was seen spectroscopically and visually between pH 4 and pH 10, exhibiting a color change from blue to pink, respectively Quite significantly, this reversible process implies a correspondence to the initial reversible stage of fibrillogenesis (step 1 in Figure 1) and may involve the structural conformation of its intermediate. It provides conformational information of the conjugated protein, giving us further insight into the intermediate structure of A at the interfacial environment
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