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
收藏
页码：9448 / 9451
页数：4
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