Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide.
Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide.
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DOI：
10.1021/acsnano.8b02346
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发表时间：
2018-06-26
期刊：
影响因子：
17.1
通讯作者：
Davis TP
中科院分区：
文献类型：
--
作者：
Pilkington EH;Gustafsson OJR;Xing Y;Hernandez-Fernaud J;Zampronio C;Kakinen A;Faridi A;Ding F;Wilson P;Ke PC;Davis TP
淀粉样蛋白可被视为在复杂蛋白质混合物存在下形成的天然纳米材料。通过与生物液体中纳米颗粒的物理化学性质进行类比，我们假设淀粉样蛋白应该在体内形成蛋白质冠，这将使潜在的淀粉样蛋白具有修饰的生物特性。为了探索这一假设，我们的特点是人胰岛淀粉样多肽（IAPP）的原纤维在FBS的蛋白质冠使用两种互补的方法，石英晶体微量天平和“离心捕获”，加上纳米液相色谱串联质谱。获得了明显的蛋白质冠的明确证据。淀粉样冠蛋白的理化性质没有发现任何趋势，而与IAPP原纤维的强结合发生在线性蛋白或具有结构可塑性的多结构域蛋白。蛋白质组学分析鉴定了富含淀粉样蛋白的蛋白质，已知这些蛋白质在介导细胞机械和加工中发挥重要作用，可能导致病理结果和治疗靶点。
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 in vivo 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 FBS using two complementary methodologies developed herein; quartz crystal microbalance and ‘centrifugal capture’, coupled with nano-liquid 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, while strong binding with IAPP fibrils occurred for linear proteins or multi-domain 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.
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