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Author

Kim, Yung Sam
Ultrafast 2D IR Spectroscopy Lab
Research Interests
  • 2D IR, chemical exchange of H-bond, fast reaction dynamics, protein dynamics

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Intrinsic Structural Heterogeneity and Long-Term Maturation of Amyloid beta Peptide Fibrils

Cited 2 times inthomson ciCited 1 times inthomson ci
Title
Intrinsic Structural Heterogeneity and Long-Term Maturation of Amyloid beta Peptide Fibrils
Author
Ma, JianqiangKomatsu, HiroakiKim, Yung SamLiu, LiuHochstrasser, Robin M.Axelsen, Paul H.
Keywords
2D infrared photon echo experiment; 13C; 18O; linear excitons; spectral crosspeaks; Stable isotopes; ultrafast vibrational laser spectroscopy
Issue Date
201308
Publisher
AMER CHEMICAL SOC
Citation
ACS CHEMICAL NEUROSCIENCE, v.4, no.8, pp.1236 - 1243
Abstract
Amyloid β peptides form fibrils that are commonly assumed to have a dry, homogeneous, and static internal structure. To examine these assumptions, fibrils under various conditions and different ages have been examined with multidimensional infrared spectroscopy. Each peptide in the fibril had a 13C=18O label in the backbone of one residue to disinguish the amide I′ absorption due to that residue from the amide I′ absorption of other residues. Fibrils examined soon after they formed, and reexamined after 1 year in the dry state, exhibited spectral changes confirming that structurally significant water molecules were present in the freshly formed fibrils. Results from fibrils incubated in solution for 4 years indicate that water molecules remained trapped within fibrils and mobile over the 4 year time span. These water molecules are structurally significant because they perturb the parallel β-sheet hydrogen bonding pattern at frequent intervals and at multiple points within individual fibrils, creating structural heterogeneity along the length of a fibril. These results show that the interface between β-sheets in an amyloid fibril is not a "dry zipper", and that the internal structure of a fibril evolves while it remains in a fibrillar state. These features, water trapping, structural heterogeneity, and structural evolution within a fibril over time, must be accommodated in models of amyloid fibril structure and formation.
URI
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DOI
http://dx.doi.org/10.1021/cn400092v
ISSN
1948-7193
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