An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure

Biochemistry ◽  
1991 ◽  
Vol 30 (43) ◽  
pp. 10382-10387 ◽  
Author(s):  
Richard G. S. Spencer ◽  
Kurt J. Halverson ◽  
Michele Auger ◽  
Ann E. McDermott ◽  
Robert G. Griffin ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Solid State ◽  
Secondary Structure ◽  
Solid State Nmr ◽  
Protein Secondary Structure ◽  
Peptide Conformation ◽  
Amyloid Formation

scholarly journals Solid-state NMR investigation of the involvement of the P2 region in tau amyloid fibrils

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Adriana Savastano ◽  
Garima Jaipuria ◽  
Loren Andreas ◽  
Eckhard Mandelkow ◽  
Markus Zweckstetter
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Fibrils ◽  
Dimensional Structure ◽  
Rich Region ◽  
Insight Into ◽  
Proline Rich Region ◽  
Tau Fibrils

AbstractThe aggregation of hyperphosphorylated tau into amyloid fibrils is closely linked to the progression of Alzheimer’s disease. To gain insight into the link between amyloid structure and disease, the three-dimensional structure of tau fibrils has been studied using solid-state NMR (ssNMR) and cryogenic electron microscopy (cryo-EM). The proline-rich region of tau remains poorly defined in the context of tau amyloid structures, despite the clustering of several phosphorylation sites, which have been associated with Alzheimer’s disease. In order to gain insight into the contribution of the proline-rich region P2 of tau to amyloid fibrils, we studied in vitro aggregated amyloid fibrils of tau constructs, which contain both the proline-rich region P2 and the pseudo-repeats. Using ssNMR we show that the sequence $$^{225}{\text {KVAVVRT}}^{231}$$ 225 KVAVVRT 231 , the most hydrophobic patch within the P2 region, loses its flexibility upon formation of amyloid fibrils. The data suggest a contribution of the P2 region to tau amyloid fibril formation, which might account for some of the unassigned electron density in cryo-EM studies of tau fibrils and could be modulated by tau phosphorylation at the disease-associated AT180 epitope T231/S235.

Solid-state NMR determination of the secondary structure of Samia cynthia ricini silk

Nature ◽  
2000 ◽  
Vol 405 (6790) ◽  
pp. 1077-1079 ◽  
Author(s):  
J. D. van Beek ◽  
L. Beaulieu ◽  
H. Schäfer ◽  
M. Demura ◽  
T. Asakura ◽  
...  
Keyword(s):  
Solid State ◽  
Secondary Structure ◽  
Solid State Nmr

scholarly journals Solid-State NMR Structural Studies of Alzheimer's Disease Aβ(1-42) And Aβ(1-40) In Phospholipid Bilayers

2010 ◽  
Vol 98 (3) ◽  
pp. 176a ◽  
Author(s):  
John D. Gehman ◽  
Raffaello Verardi ◽  
Anil K. Mehta ◽  
Gianluigi Veglia ◽  
Frances Separovic
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Solid State ◽  
Solid State Nmr ◽  
Phospholipid Bilayers ◽  
Structural Studies

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

Quantification of protein secondary structure by 13C solid-state NMR

2016 ◽  
Vol 408 (14) ◽  
pp. 3875-3879 ◽  
Author(s):  
Fabiana Diuk Andrade ◽  
Lucimara Aparecida Forato ◽  
Rubens Bernardes Filho ◽  
Luiz Alberto Colnago
Keyword(s):  
Solid State ◽  
Secondary Structure ◽  
Solid State Nmr ◽  
Protein Secondary Structure
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