1 research outputs found
Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide
Amyloids
may be regarded as native nanomaterials that form in the
presence of complex protein mixtures. By drawing an analogy with the
physicochemical properties of nanoparticles in biological fluids,
we hypothesized that amyloids should form a protein corona <i>in vivo</i> that would imbue the underlying amyloid with a modified
biological identity. To explore this hypothesis, we characterized
the protein corona of human islet amyloid polypeptide (IAPP) fibrils
in fetal bovine serum using two complementary methodologies developed
herein: quartz crystal microbalance and “centrifugal capture”,
coupled with nanoliquid chromatography tandem mass spectroscopy. Clear
evidence for a significant protein corona was obtained. No trends
were identified for amyloid corona proteins based on their physicochemical
properties, whereas strong binding with IAPP fibrils occurred for
linear proteins or multidomain proteins with structural plasticity.
Proteomic analysis identified amyloid-enriched proteins that are known
to play significant roles in mediating cellular machinery and processing,
potentially leading to pathological outcomes and therapeutic targets