Metastability of native proteins and the phenomenon of amyloid formation.

An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils reveals that this structural form is likely to be the most stable one that protein molecules can adopt even under physiological conditions. This result challenges the conventional assumption that functional forms of proteins correspond to the global minima in their free energy surfaces and suggests that living systems are conformationally as well as chemically metastable.

[1]  Alma L. Burlingame,et al.  Widespread Protein Aggregation as an Inherent Part of Aging in C. elegans , 2010, PLoS biology.

[2]  Andrew D. Ellington,et al.  Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation , 2009, Proceedings of the National Academy of Sciences.

[3]  N. Grigorieff,et al.  Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy , 2008, Proceedings of the National Academy of Sciences.

[4]  Beat H. Meier,et al.  Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core , 2008, Science.

[5]  Michele Vendruscolo,et al.  Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils , 2007, Science.

[6]  Michele Vendruscolo,et al.  Life on the edge: a link between gene expression levels and aggregation rates of human proteins. , 2007, Trends in biochemical sciences.

[7]  R. Wetzel,et al.  Polymorphism in the intermediates and products of amyloid assembly. , 2007, Current opinion in structural biology.

[8]  D. Selkoe,et al.  Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide , 2007, Nature Reviews Molecular Cell Biology.

[9]  C. Dobson,et al.  Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.

[10]  Ronald Wetzel,et al.  Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stability. , 2006, Journal of molecular biology.

[11]  R. Tycko,et al.  Molecular structure of amyloid fibrils: insights from solid-state NMR , 2006, Quarterly Reviews of Biophysics.

[12]  R. Wetzel,et al.  Thermodynamics of Aβ(1−40) Amyloid Fibril Elongation† , 2005 .

[13]  刘金明,et al.  IL-13受体α2降低血吸虫病肉芽肿的炎症反应并延长宿主存活时间[英]/Mentink-Kane MM,Cheever AW,Thompson RW,et al//Proc Natl Acad Sci U S A , 2005 .

[14]  Christopher M. Dobson,et al.  Molecular recycling within amyloid fibrils , 2005, Nature.

[15]  David Barlam,et al.  Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures. , 2005, Nano letters.

[16]  Yuji Goto,et al.  Direct Measurement of the Thermodynamic Parameters of Amyloid Formation by Isothermal Titration Calorimetry* , 2004, Journal of Biological Chemistry.

[17]  Kazumasa Sakurai,et al.  Conformational stability of amyloid fibrils of β2‐microglobulin probed by guanidine‐hydrochloride‐induced unfolding , 2004, FEBS letters.

[18]  Daryi Wang,et al.  A general tendency for conservation of protein length across eukaryotic kingdoms. , 2004, Molecular biology and evolution.

[19]  C. Dobson Protein folding and misfolding , 2003, Nature.

[20]  V. Morozov,et al.  Effect of exercise to exhaustion on myeloperoxidase and lysozyme release from blood neutrophils , 2003, European Journal of Applied Physiology.

[21]  C. Dobson,et al.  Preparation and characterization of purified amyloid fibrils. , 2001, Journal of the American Chemical Society.

[22]  J. V. Moran,et al.  Initial sequencing and analysis of the human genome. , 2001, Nature.

[23]  E. Cota,et al.  Folding studies of immunoglobulin-like beta-sandwich proteins suggest that they share a common folding pathway. , 1999, Structure.

[24]  C. Dobson Protein misfolding, evolution and disease. , 1999, Trends in biochemical sciences.

[25]  A. Fersht Structure and mechanism in protein science , 1998 .

[26]  P. Wolynes,et al.  Spin glasses and the statistical mechanics of protein folding. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[27]  B. Derrida Random-energy model: An exactly solvable model of disordered systems , 1981 .

[28]  P. Walter,et al.  Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway. , 2001, Molecular biology of the cell.

[29]  A. R. Fresht Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding , 1999 .

[30]  F. Oosawa,et al.  A theory of linear and helical aggregations of macromolecules. , 1962, Journal of molecular biology.