Characterizing Early Aggregates Formed by an Amyloidogenic Peptide by Mass Spectrometry

被引：30

作者：

Cole, Harriet L. ^{[2
]}

Kalapothakis, Jason M. D. ^{[1
]}

Bennett, Guy ^{[1
]}

Barran, Perdita E. ^{[1
]}

MacPhee, Cait E. ^{[2
]}

机构：

[1] Univ Edinburgh, Sch Chem, Edinburgh EH9 3JJ, Midlothian, Scotland

[2] Univ Edinburgh, Sch Phys & Astron, SUPA, JCMB, Edinburgh EH9 3JZ, Midlothian, Scotland

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 49期

基金：

英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

amyloids; ion mobility; mass spectrometry; oligomers; polypeptides; BETA-PROTEIN OLIGOMERIZATION; ION MOBILITY MEASUREMENTS; FIBRIL FORMATION; INFORMATION; A-BETA-42; CLUSTERS; STATES;

D O I：

10.1002/anie.201003373

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

What floats in the soup? Time-course and ion-mobility nano-electrospray ionization (nESI) mass spectrometry probes the early aggregation states of an amyloidogenic endecapeptide derived from amino acid residues 105-115 of the human plasma protein transthyretin. A wide range of densely packed prefibrillar oligomers 1 ≤ n ≤ 13 are observed in dynamic populations over 8 h. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：9448 / 9451

页数：4

共 24 条

[1] Cytochrome display on amyloid fibrils
Baldwin, AJ
Bader, R
Christodoulou, J
MacPhee, CE
Dobson, CM
Barker, PD
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (07) : 2162 - 2163
[2] Amyloid β-protein:: Monomer structure and early aggregation states of Aβ42 and its Pro19 alloform
Bernstein, SL
Wyttenbach, T
Baumketner, A
Shea, JE
Bitan, G
Teplow, DB
Bowers, MT
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (07) : 2075 - 2084
[3] Bernstein SL, 2004, J AM SOC MASS SPECTR, V15, P1435, DOI [10.1016/j.jasms.2004.08.003, 10.1016/j.jasms.2004.05.003]
[4] Bernstein SL, 2009, NAT CHEM, V1, P326, DOI [10.1038/nchem.247, 10.1038/NCHEM.247]
[5] Amyloid β-protein (Aβ) assembly:: Aβ40 and Aβ42 oligomerize through distinct pathways
Bitan, G
Kirkitadze, MD
Lomakin, A
Vollers, SS
Benedek, GB
Teplow, DB
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (01) : 330 - 335
[6] Amyloid β-protein oligomerization -: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
Bitan, G
Lomakin, A
Teplow, DB
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (37) : 35176 - 35184
[7] Possibilities for 'smart' materials exploiting the self-assembly of polypeptides into fibrils
Channon, Kevin
MacPhee, Cait E.
[J]. SOFT MATTER, 2008, 4 (04) : 647 - 652
[8] Clemmer DE, 1997, J MASS SPECTROM, V32, P577
[9] Oligomers of the Prion Protein Fragment 106-126 Are Likely Assembled from β-Hairpins in Solution, and Methionine Oxidation Inhibits Assembly without Altering the Peptide's Monomeric Conformation
Grabenauer, Megan
Wu, Chun
Soto, Patricia
Shea, Joan-Emma
Bowers, Michael T.
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2010, 132 (02) : 532 - 539
[10] High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
Jaroniec, CP
MacPhee, CE
Bajaj, VS
McMahon, MT
Dobson, CM
Griffin, RG
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (03) : 711 - 716

← 1 2 3 →