Kinetic intermediates in amyloid assembly

Chen Liang; Rong Ni; Jillian E. Smith-Carpenter; W. Seth Childers; Anil K. Mehta; David G. Lynn

doi:10.1021/ja508621b

Kinetic intermediates in amyloid assembly

Chen Liang
, Rong Ni
, Jillian E. Smith-Carpenter
, W. Seth Childers
, Anil K. Mehta
, David G. Lynn

Fairfield University

Research output: Contribution to journal › Article › peer-review

Abstract

In contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the Aβ peptide of Alzheimer’s disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.

Original language	American English
Journal	Journal of the American Chemical Society
Volume	136
DOIs	https://doi.org/10.1021/ja508621b
State	Published - Jan 1 2014

Disciplines

Chemistry
Physical Sciences and Mathematics

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Kinetic intermediates in amyloid assemblyFinal published version, 1.71 MBLicense: CC BY

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title = "Kinetic intermediates in amyloid assembly",

abstract = " In contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the Aβ peptide of Alzheimer{\textquoteright}s disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.",

author = "Chen Liang and Rong Ni and Smith-Carpenter, \{Jillian E.\} and Childers, \{W. Seth\} and Mehta, \{Anil K.\} and Lynn, \{David G.\}",

year = "2014",

month = jan,

day = "1",

doi = "10.1021/ja508621b",

language = "American English",

volume = "136",

journal = "Journal of the American Chemical Society",

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T1 - Kinetic intermediates in amyloid assembly

AU - Liang, Chen

AU - Ni, Rong

AU - Smith-Carpenter, Jillian E.

AU - Childers, W. Seth

AU - Mehta, Anil K.

AU - Lynn, David G.

PY - 2014/1/1

Y1 - 2014/1/1

N2 - In contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the Aβ peptide of Alzheimer’s disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.

AB - In contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the Aβ peptide of Alzheimer’s disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.

UR - https://digitalcommons.fairfield.edu/chemistry-facultypubs/23

U2 - 10.1021/ja508621b

DO - 10.1021/ja508621b

M3 - Article

VL - 136

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

ER -

Kinetic intermediates in amyloid assembly

Abstract

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