https://scholars.lib.ntu.edu.tw/handle/123456789/407270
標題: | Fibrillization of β-Amyloid Peptides via Chemically Modulated Pathway | 作者: | Guo, Z.-H. Yang, C.-I. Ho, C.-I. Huang, S.-J. Chen, Y.-C. Tai, H.-C. Chan, J.C.C. |
公開日期: | 2018 | 卷: | 24 | 期: | 19 | 起(迄)頁: | 4939-4943 | 來源出版物: | Chemistry - A European Journal | 摘要: | The aggregation of β-amyloid peptides is closely associated with Alzheimer's disease. We have used liposomes to modulate the early aggregation events of 40-residue β-amyloid peptides. The spatial confinement provided by liposomes leads to the formation of nonfibrillar aggregates of β-amyloid peptides. These on-pathway β-sheet intermediates were used to seed the fibrillization of the monomer peptides. Solid-state NMR spectroscopy revealed that the resultant fibrils have a more uniform structure than those formed in liposome-free solution. ? 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85042767118&doi=10.1002%2fchem.201706001&partnerID=40&md5=1300a585a9c4ced6ac213cf972afea4d https://scholars.lib.ntu.edu.tw/handle/123456789/407270 |
DOI: | 10.1002/chem.201706001 | SDG/關鍵字: | Glycoproteins; Liposomes; Neurodegenerative diseases; Nuclear magnetic resonance spectroscopy; Nucleation; Peptides; Polymorphism; Self assembly; Alzheimer's disease; Beta amyloid peptides; Fibrillization; Peptidic fibrils; Seeding effects; Solid-state NMR spectroscopy; Spatial confinement; Uniform structure; Proteins; amyloid beta protein; liposome; peptide; Alzheimer disease; chemistry; cytoskeleton; human; protein secondary structure; Alzheimer Disease; Amyloid beta-Peptides; Cytoskeleton; Humans; Liposomes; Peptides; Protein Structure, Secondary |
顯示於: | 化學系 |
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