Association of amyloid-β peptide with membrane surfaces monitored by solid state NMR

2002 ◽  
Vol 4 (22) ◽  
pp. 5524-5530 ◽  
Author(s):  
Fredrick Lindström ◽  
Marcus Bokvist ◽  
Tobias Sparrman ◽  
Gerhard Gröbner
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Membrane Surfaces

Application of DNP-enhanced solid-state NMR to studies of amyloid-β peptide interaction with lipid membranes

2021 ◽  
Vol 236 ◽  
pp. 105071
Author(s):  
Thomas Deo ◽  
Qinghui Cheng ◽  
Subhadip Paul ◽  
Wei Qiang ◽  
Alexey Potapov
Keyword(s):  
Solid State ◽  
Lipid Membranes ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Interaction

scholarly journals Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-β peptide: perspectives for DNP

2013 ◽  
Vol 56 (4) ◽  
pp. 359-363 ◽  
Author(s):  
Juan-Miguel Lopez del Amo ◽  
Dennis Schneider ◽  
Antoine Loquet ◽  
Adam Lange ◽  
Bernd Reif
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Nmr Studies

scholarly journals Solid-state NMR sequential assignment of an Amyloid-β(1–42) fibril polymorph

2016 ◽  
Vol 10 (2) ◽  
pp. 269-276 ◽  
Author(s):  
Francesco Ravotti ◽  
Marielle Aulikki Wälti ◽  
Peter Güntert ◽  
Roland Riek ◽  
Anja Böckmann ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Sequential Assignment

scholarly journals Solid-state NMR Reveals a Close Structural Relationship between Amyloid-β Protofibrils and Oligomers

2012 ◽  
Vol 287 (27) ◽  
pp. 22822-22826 ◽  
Author(s):  
Holger A. Scheidt ◽  
Isabel Morgado ◽  
Daniel Huster
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Structural Relationship

scholarly journals Out-of-register parallel β-sheets and antiparallel β-sheets coexist in 150 kDa oligomers formed by Aβ(1-42)

2020 ◽  
Author(s):  
Yuan Gao ◽  
Cong Guo ◽  
Jens O. Watzlawik ◽  
Elizabeth J. Lee ◽  
Danting Huang ◽  
...  
Keyword(s):  
Solid State Nmr ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Dipolar Recoupling ◽  
Negative Results ◽  
Assembly Pathway ◽  
Fibril Structure ◽  
Proposed Model ◽  
Β Sheets ◽  
Β Sheet

AbstractWe present solid-state NMR measurements of β-strand secondary structure and inter-strand organization within a 150 kDa oligomeric aggregate of the 42-residue variant of the Alzheimer’s amyloid-β peptide (Aβ(1-42)). This oligomer is characterized by a structure that cannot be explained by any previously proposed model for aggregated Aβ. We build upon our previous report of a β-strand spanned by residues 30-42, which arranges into an antiparallel β-sheet. New results presented here indicate that there is a second β-strand formed by residues 11-24. We show negative results for NMR experiments designed to reveal antiparallel β-sheets formed by this β-strand. Remarkably, we show that this strand is organized into a parallel β-sheet despite the co-existence of an antiparallel β-sheet in the same structure. In addition, the in-register parallel β-sheet commonly observed for amyloid fibril structure does not apply to residues 11-24 in the 150 kDa oligomer. Rather, we present evidence for an inter-strand registry shift of 3 residues that alternates in direction between adjacent molecules along the β-sheet. We corroborated this unexpected scheme for β-strand organization using multiple 2-dimensional NMR and 13C-13C dipolar recoupling experiments. Our findings indicate a previously unknown assembly pathway and inspire a suggestion as to why this aggregate does not grow to larger sizes.

scholarly journals Structural characteristics of oligomers formed by pyroglutamate-modified amyloid β peptides studied by solid-state NMR

2020 ◽  
Vol 22 (29) ◽  
pp. 16887-16895 ◽  
Author(s):  
Holger A. Scheidt ◽  
Anirban Das ◽  
Alexander Korn ◽  
Martin Krueger ◽  
Sudipta Maiti ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Structural Characteristics ◽  
Amyloid Β ◽  
Wild Type

Structure of oligomers of truncated and pyroglutamate modified amyloid β variants is similar to the wild type.

scholarly journals Structural Insight into an Alzheimer’s Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR

2015 ◽  
Vol 137 (20) ◽  
pp. 6480-6483 ◽  
Author(s):  
Sudhakar Parthasarathy ◽  
Masafumi Inoue ◽  
Yiling Xiao ◽  
Yoshitaka Matsumura ◽  
Yo-ichi Nabeshima ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Structural Insight ◽  
Insight Into
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