淀粉样蛋白纤维微观结构的红外光谱分析
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- 英文论文题名：Amyloid Fibril Structural Analysis by Infrared Spectroscopy
- 论文作者：马刚 ; 高亚超 ; 邹烨 ; 李昊一
- 英文论文作者：Gang Ma ; Yachao Gao ; Ye Zou ; Haoyi Li ; Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education ; College of Chemistry and Environmental Science ; Hebei University
- 年：2016
- 作者机构：河北大学化学与环境科学学院药物化学与分子诊断教育部重点实验室;
- 论文关键词：淀粉样蛋白 ; 蛋白纤维化 ; 红外光谱 ; 红外光谱探针
- 会议召开时间：2016-07-01
- 会议录名称：中国化学会第30届学术年会摘要集-第二十八分会：化学生物学
- 语种：中文
- 分类号：O657.33;O636
- 学会代码：ZGHY
- 会议名称：中国化学会第30届学术年会-第二十八分会 ; 化学生物学
- 会议地点：中国辽宁大连
- 主办单位：中国化学会
- 学会名称：中国化学会
- 页数：1
- 文件大小：226k
- 原文格式：D
- 会议级别：全国
摘要
淀粉样蛋白纤维是一种具有独特微观结构的蛋白聚集体。就微观形貌而言,淀粉样蛋白纤维是宽度为纳米级而长度可达微米级的蛋白纳米线;就空间构型而言,淀粉样蛋白纤维是由至少两个β-折叠片层以非共价键形式结合而形成的具有cross-β结构的超分子体系~([1])。淀粉样蛋白纤维由于与包括阿尔茨海默病和帕金森病在内的几十种威胁人类健康的疾病密切相关而被广为关注~([2])。淀粉样蛋白纤维的微观结构解析对于发展以淀粉样结构为靶点的相关疾病治疗药物至关重要。本研究中,我们致力于应用傅里叶变换红外光谱并结合红外光谱探针技术对淀粉样蛋白纤维的微观结构进行解析。我们首先提出红外光谱技术可以用来判别淀粉样蛋白纤维中多肽链的具体β-折叠构型,并详细探讨了判断平行和反平行β-折叠构型的红外光谱判据。之后,我们描述了一种对淀粉样多肽进行硫氰酸基红外光谱探针标记的化学方法。最后,我们展示了常规红外光谱结合红外光谱探针技术在淀粉样蛋白纤维结构解析中的应用潜力。
Amyloid fibrils are unique type of protein aggregates featuring fibrillar nanoscale morphology and cross-β supramolecular architecture.In vivo,amyloid fibrils are associated with dozens of serious human diseases including the well-known Alzheimer's disease and Parkinson's disease.Elucidating the structure of amyloid fibril is crucial in the drug discovery of amyloid-related diseases.Here,we report how the conventional infrared spectroscopy in combination with novel infrared probe technique can be employed to reveal the detailed microscopic structural feature of amyloid fibril.In addition,we will discuss the infrared assignment criteria for parallel and antiparallel β-sheets;and will describe a method to incorporate a thiocyanate infrared probe onto amyloidogenic peptides.
Amyloid fibrils are unique type of protein aggregates featuring fibrillar nanoscale morphology and cross-β supramolecular architecture.In vivo,amyloid fibrils are associated with dozens of serious human diseases including the well-known Alzheimer's disease and Parkinson's disease.Elucidating the structure of amyloid fibril is crucial in the drug discovery of amyloid-related diseases.Here,we report how the conventional infrared spectroscopy in combination with novel infrared probe technique can be employed to reveal the detailed microscopic structural feature of amyloid fibril.In addition,we will discuss the infrared assignment criteria for parallel and antiparallel β-sheets;and will describe a method to incorporate a thiocyanate infrared probe onto amyloidogenic peptides.
引文
[1]Sawaya,M.R.;Sambashivan,S.;Nelson,R.;Ivanova,M.I.;Sievers,S.A.;Apostol,M.I.;Thompson,M.J.;Balbirnie,M.;Wiltzius,J.J.W.;McFarlane,H.T.;Madsen,A.O.;Riekel,C.;Eisenberg,D.Nature 2007,447:453.
[2]Chiti,F.;Dobson,C.M.Annu.Rev.Biochem.2006,75:333.
[2]Chiti,F.;Dobson,C.M.Annu.Rev.Biochem.2006,75:333.