Fibrillization of β-Amyloid Peptides via Chemically Modulated Pathway

被引：2

作者：

Guo, Zhong-Hong ^{[1
]}

Yang, Chien-I ^{[1
]}

Ho, Cheng-I ^{[1
]}

Huang, Shing-Jong ^{[2
]}

Chen, Yin-Chung ^{[1
]}

Tai, Hwan-Ching ^{[1
]}

Chan, Jerry Chun Chung ^{[1
]}

机构：

[1] Natl Taiwan Univ, Dept Chem, 1,Sect 4,Roosevelt Rd, Taipei 10617, Taiwan

[2] Natl Taiwan Univ, Instrumentat Ctr, 1,Sect 4,Roosevelt Rd, Taipei 10617, Taiwan

来源：

CHEMISTRY-A EUROPEAN JOURNAL | 2018年 / 24卷 / 19期

关键词：

Alzheimer's disease; nucleation; peptides; peptidic fibrils; polymorphism; seeding effects; ALZHEIMERS-DISEASE; STRUCTURAL BASIS; MOLECULAR-STRUCTURE; FIBRIL FORMATION; A-BETA; POLYMORPHISM; KINETICS; STATE; AGGREGATION;

D O I：

10.1002/chem.201706001

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The aggregation of beta-amyloid peptides is closely associated with Alzheimer's disease. We have used liposomes to modulate the early aggregation events of 40-residue beta-amyloid peptides. The spatial confinement provided by liposomes leads to the formation of nonfibrillar aggregates of beta amyloid peptides. These on-pathway beta-sheet intermediates were used to seed the fibrillization of the monomer peptides. Solid-state NMR spectroscopy revealed that the resultant fibrils have a more uniform structure than those formed in liposome-free solution.

引用

页码：4939 / 4943

页数：5

共 38 条

[1] Adjustable twisting periodic pitch of amyloid fibrils [J].

Adamcik, Jozef ;

Mezzenga, Raffaele .

SOFT MATTER, 2011, 7 (11) :5437-5443

[2] Protein misfolding, functional amyloid, and human disease [J].

Chiti, Fabrizio ;

Dobson, Christopher M. .

ANNUAL REVIEW OF BIOCHEMISTRY, 2006, 75 :333-366

[3] Endocytosis is required for synaptic activity-dependent release of amyloid-β in vivo [J].

Cirrito, John R. ;

Kang, Jae-Eun ;

Lee, Jiyeon ;

Stewart, Floy R. ;

Verges, Deborah K. ;

Silverio, Luz M. ;

Bu, Guojun ;

Mennerick, Steven ;

Holtzman, David M. .

NEURON, 2008, 58 (01) :42-51

[4] Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments [J].

Cohen, Samuel I. A. ;

Vendruscolo, Michele ;

Welland, Mark E. ;

Dobson, Christopher M. ;

Terentjev, Eugene M. ;

Knowles, Tuomas P. J. .

JOURNAL OF CHEMICAL PHYSICS, 2011, 135 (06)

[5]

Fändrich M, 2009, PRION, V3, P89

[6] CALCULATION OF PROTEIN EXTINCTION COEFFICIENTS FROM AMINO-ACID SEQUENCE DATA [J].

GILL, SC ;

VONHIPPEL, PH .

ANALYTICAL BIOCHEMISTRY, 1989, 182 (02) :319-326

[7] Studies on the in vitro assembly of Aβ 1-40:: Implications for the search for Aβ fibril formation inhibitors [J].

Goldsbury, CS ;

Wirtz, S ;

Müller, SA ;

Sunderji, S ;

Wicki, P ;

Aebi, U ;

Frey, P .

JOURNAL OF STRUCTURAL BIOLOGY, 2000, 130 (2-3) :217-231

[8] Fibril structure of amyloid-β(1-42) by cryo-electron microscopy [J].

Gremer, Lothar ;

Schoelzel, Daniel ;

Schenk, Carla ;

Reinartz, Elke ;

Labahn, Joerg ;

Ravelli, Raimond B. G. ;

Tusche, Markus ;

Lopez-Iglesias, Carmen ;

Hoyer, Wolfgang ;

Heise, Henrike ;

Willbold, Dieter ;

Schroeder, Gunnar F. .

SCIENCE, 2017, 358 (6359) :116-+

[9] The Amyloid Beta Peptide: A Chemist's Perspective. Role in Alzheimer's and Fibrillization [J].

Hamley, I. W. .

CHEMICAL REVIEWS, 2012, 112 (10) :5147-5192

[10] The protofilament structure of insulin amyloid fibrils [J].

Jimenez, JL ;

Nettleton, EJ ;

Bouchard, M ;

Robinson, CV ;

Dobson, CM ;

Saibil, HR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (14) :9196-9201

← 1 2 3 4 →