Guo, Z.-H.Z.-H.GuoYang, C.-I.C.-I.YangHo, C.-I.C.-I.HoHuang, S.-J.S.-J.HuangChen, Y.-C.Y.-C.ChenTai, H.-C.H.-C.TaiChan, J.C.C.J.C.C.Chan2019-05-102019-05-102018https://www.scopus.com/inward/record.uri?eid=2-s2.0-85042767118&doi=10.1002%2fchem.201706001&partnerID=40&md5=1300a585a9c4ced6ac213cf972afea4dhttps://scholars.lib.ntu.edu.tw/handle/123456789/407270The 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[SDGs]SDG3Glycoproteins; 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, Secondaryjournal article10.1002/chem.2017060012-s2.0-85042767118