Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 29, Pages 8435-8439Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201501981
Keywords
amyloid beta; NMR spectroscopy; self-assembly; sugar cluster; alpha-synuclein
Categories
Funding
- JST
- ACCEL
- KAKENHI [24685010, 25102007, 25102001, 25102008, 15K21680, 26560451]
- National Center for Geriatrics and Gerontology [25-19]
- Okazaki ORION project
- Nanotechnology Network Project
- Nanotechnology Platform Program at IMS
- Grants-in-Aid for Scientific Research [15K21680, 25102001, 24685010, 26560451, 25102007] Funding Source: KAKEN
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Physiological and pathological functions of glycans are promoted through their clustering effects as exemplified by a series of gangliosides, sialylated glycosphingolipids, which serve as acceptors for bacterial toxins and viruses. Furthermore, ganglioside GM1 clusters on neuronal cell membranes specifically interact with amyloidogenic proteins, triggering their conformational transitions and leading to neurodegeneration. Here we develop a self-assembled spherical complex that displays a cluster of the GM1 pentasaccharide, and successfully demonstrate its ability to interact with amyloid beta and alpha-synuclein. Due to the lack of hydrophobic lipid moieties, which would stably trap these cohesive proteins or give rise to toxic aggregates, this artificial cluster enabled NMR spectroscopic characterization of the early encounter stage of protein interactions with its outer carbohydrate moieties, which were not observable with previous glycan clusters.
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