Amyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape

被引:264
作者
Adamcik, Jozef [1 ]
Mezzenga, Raffaele [1 ,2 ]
机构
[1] Swiss Fed Inst Technol, Dept Hlth Sci & Technol, Schmelzbergstr 9, CH-8092 Zurich, Switzerland
[2] Swiss Fed Inst Technol, Dept Mat, Wolfgang Pauli Str 10, CH-8093 Zurich, Switzerland
关键词
amyloids; energy landscapes; polymorphism; protein aggregation; protein folding; SOLID-STATE NMR; ATOMIC-FORCE MICROSCOPY; BETA-SHEET STRUCTURE; IN-VIVO; STRUCTURAL BASIS; MOLECULAR-LEVEL; ELECTRON-MICROSCOPY; CHAPERONE MACHINES; GLOBULAR-PROTEINS; FORMING PEPTIDE;
D O I
10.1002/anie.201713416
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Protein folding involves a large number of steps and conformations in which the folding protein samples different thermodynamic states characterized by local minima. Kinetically trapped on- or off-pathway intermediates are metastable folding intermediates towards the lowest absolute energy minima, which have been postulated to be the natively folded state where intramolecular interactions dominate, and the amyloid state where intermolecular interactions dominate. However, this view largely neglects the rich polymorphism found within amyloid species. We review the protein folding energy landscape in view of recent findings identifying specific transition routes among different amyloid polymorphs. Observed transitions such as twisted ribboncrystal or helical ribbonnanotube, and forbidden transitions such helical ribbon?crystal, are discussed and positioned within the protein folding and aggregation energy landscape. Finally, amyloid crystals are identified as the ground state of the protein folding and aggregation energy landscape.
引用
收藏
页码:8370 / 8382
页数:13
相关论文
共 113 条
[1]  
Adamcik J., 2011, ANGEW CHEM, V123, P5609
[2]  
Adamcik J., 2016, Angewandte Chemie, V128, P628
[3]   Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons [J].
Adamcik, Jozef ;
Sanchez-Ferrer, Antoni ;
Ait-Bouziad, Nadine ;
Reynolds, Nicholas P. ;
Lashuel, Hilal A. ;
Mezzenga, Raffaele .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2016, 55 (02) :618-622
[4]   Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method [J].
Adamcik, Jozef ;
Lara, Cecile ;
Usov, Ivan ;
Jeong, Jae Sun ;
Ruggeri, Francesco S. ;
Dietler, Giovanni ;
Lashuel, Hilal A. ;
Hamley, Ian W. ;
Mezzenga, Raffaele .
NANOSCALE, 2012, 4 (15) :4426-4429
[5]   Proteins Fibrils from a Polymer Physics Perspective [J].
Adamcik, Jozef ;
Mezzenga, Raffaele .
MACROMOLECULES, 2012, 45 (03) :1137-1150
[6]   Direct Observation of Time-Resolved Polymorphic States in the Self-Assembly of End-Capped Heptapeptides [J].
Adamcik, Jozef ;
Castelletto, Valeria ;
Bolisetty, Sreenath ;
Hamley, Ian W. ;
Mezzenga, Raffaele .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2011, 50 (24) :5495-5498
[7]  
Adamcik J, 2010, NAT NANOTECHNOL, V5, P423, DOI [10.1038/nnano.2010.59, 10.1038/NNANO.2010.59]
[8]   Hierarchical self-assembly of chiral rod-like molecules as a model for peptide β-sheet tapes, ribbons, fibrils, and fibers [J].
Aggeli, A ;
Nyrkova, IA ;
Bell, M ;
Harding, R ;
Carrick, L ;
McLeish, TCB ;
Semenov, AN ;
Boden, N .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (21) :11857-11862
[9]   PRINCIPLES THAT GOVERN FOLDING OF PROTEIN CHAINS [J].
ANFINSEN, CB .
SCIENCE, 1973, 181 (4096) :223-230
[10]  
Annamalai K., 2016, ANGEW CHEM, V128, P4903