scholarly journals Linking Protein Folding to Amyloid Formation

2021 ◽  
Vol 61 (6) ◽  
pp. 358-365
Author(s):  
Masahiro NOJI ◽  
Yuji GOTO
Keyword(s):  
Protein Folding ◽  
Amyloid Formation

O2-06-01 Protein folding and amyloid formation: studies on poly(L-alanine) and poly(L-glutamine)

2004 ◽  
Vol 25 ◽  
pp. S43
Author(s):  
Daniel A. Kirschner ◽  
Leonid M. Shinchuk ◽  
Natalia Reixach ◽  
Sylvie E. Blondelle ◽  
Ronald Wetzel ◽  
...  
Keyword(s):  
Protein Folding ◽  
Amyloid Formation

scholarly journals Chemical Strategies for Controlling Protein Folding and Elucidating the Molecular Mechanisms of Amyloid Formation and Toxicity

2012 ◽  
Vol 421 (2-3) ◽  
pp. 204-236 ◽  
Author(s):  
Sara Butterfield ◽  
Mirva Hejjaoui ◽  
Bruno Fauvet ◽  
Loay Awad ◽  
Hilal A. Lashuel
Keyword(s):  
Protein Folding ◽  
Molecular Mechanisms ◽  
Amyloid Formation ◽  
Chemical Strategies

Solvent Perturbation of Protein Structures - A Review Study with Lectins

2020 ◽  
Vol 27 (6) ◽  
pp. 538-550 ◽  
Author(s):  
Pritha Mandal ◽  
Anisur R. Molla
Keyword(s):  
Protein Folding ◽  
Protein Structures ◽  
Research Area ◽  
Model Systems ◽  
Amyloid Formation ◽  
Lectin Family ◽  
Review Study ◽  
Induced Structure ◽  
Structure Of Proteins

Use of organic molecules as co-solvent with water, the ubiquitous biological solvent, to perturb the structure of proteins is popular in the research area of protein structure and folding. These organic co-solvents are believed to somehow mimic the environment near the cell membrane. Apart from that they induce non-native states which can be present in the protein folding pathway or those states also may be representative of the off pathway structures leading to amyloid formation, responsible for various fatal diseases. In this review, we shall focus on organic co-solvent induced structure perturbation of various members of lectin family. Lectins are excellent model systems for protein folding study because of its wide occurrence, diverse structure and versatile biological functions. Lectins were mainly perturbed by two fluoroalcohols – 2,2,2- trifluoroethanol and 1,1,1,3,3,3-hexafluoroisopropanol whereas glycerol, ethylene glycol and polyethylene glycols were used in some cases. Overall, all native lectins were denatured by alcohols and most of the denatured lectins have predominant helical secondary structure. But characterization of the helical states and the transition pathway for various lectins revealed diverse result.

scholarly journals A Simple Lattice Model That Captures Protein Folding, Aggregation and Amyloid Formation

PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e85185 ◽  
Author(s):  
Sanne Abeln ◽  
Michele Vendruscolo ◽  
Christopher M. Dobson ◽  
Daan Frenkel
Keyword(s):  
Protein Folding ◽  
Lattice Model ◽  
Amyloid Formation ◽  
Simple Lattice

scholarly journals Preventing fibril formation of a protein by selective mutation

2015 ◽  
Vol 112 (44) ◽  
pp. 13549-13554 ◽  
Author(s):  
Gia G. Maisuradze ◽  
Jordi Medina ◽  
Khatuna Kachlishvili ◽  
Pawel Krupa ◽  
Magdalena A. Mozolewska ◽  
...  
Keyword(s):  
Protein Folding ◽  
Intermediate State ◽  
Collapse Mechanism ◽  
Amyloid Formation ◽  
Significant Delay ◽  
Ww Domain ◽  
Downhill Folding ◽  
Hydrophobic Collapse ◽  
High Resolution Nmr ◽  
Selective Mutation

The origins of formation of an intermediate state involved in amyloid formation and ways to prevent it are illustrated with the example of the Formin binding protein 28 (FBP28) WW domain, which folds with biphasic kinetics. Molecular dynamics of protein folding trajectories are used to examine local and global motions and the time dependence of formation of contacts between Cαs and Cβs of selected pairs of residues. Focus is placed on the WT FBP28 WW domain and its six mutants (L26D, L26E, L26W, E27Y, T29D, and T29Y), which have structures that are determined by high-resolution NMR spectroscopy. The origins of formation of an intermediate state are elucidated, viz. as formation of hairpin 1 by a hydrophobic collapse mechanism causing significant delay of formation of both hairpins, especially hairpin 2, which facilitates the emergence of an intermediate state. It seems that three-state folding is a major folding scenario for all six mutants and WT. Additionally, two-state and downhill folding scenarios were identified in ∼15% of the folding trajectories for L26D and L26W, in which both hairpins are formed by the Matheson–Scheraga mechanism much faster than in three-state folding. These results indicate that formation of hairpins connecting two antiparallel β-strands determines overall folding. The correlations between the local and global motions identified for all folding trajectories lead to the identification of the residues making the main contributions in the formation of the intermediate state. The presented findings may provide an understanding of protein folding intermediates in general and lead to a procedure for their prevention.

scholarly journals Breakdown of supersaturation barrier links protein folding to amyloid formation

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Masahiro Noji ◽  
Tatsushi Samejima ◽  
Keiichi Yamaguchi ◽  
Masatomo So ◽  
Keisuke Yuzu ◽  
...  
Keyword(s):  
Free Energy ◽  
Protein Folding ◽  
Amino Acid ◽  
Amyloid Fibrils ◽  
Globular Proteins ◽  
General Concept ◽  
Amyloid Formation ◽  
Energy Minimum ◽  
Native Structure ◽  
Parkinson’S Diseases

AbstractThe thermodynamic hypothesis of protein folding, known as the “Anfinsen’s dogma” states that the native structure of a protein represents a free energy minimum determined by the amino acid sequence. However, inconsistent with the Anfinsen’s dogma, globular proteins can misfold to form amyloid fibrils, which are ordered aggregates associated with diseases such as Alzheimer’s and Parkinson’s diseases. Here, we present a general concept for the link between folding and misfolding. We tested the accessibility of the amyloid state for various proteins upon heating and agitation. Many of them showed Anfinsen-like reversible unfolding upon heating, but formed amyloid fibrils upon agitation at high temperatures. We show that folding and amyloid formation are separated by the supersaturation barrier of a protein. Its breakdown is required to shift the protein to the amyloid pathway. Thus, the breakdown of supersaturation links the Anfinsen’s intramolecular folding universe and the intermolecular misfolding universe.

Sign in / Sign up

Export Citation Format

Share Document