Literature DB >> 20866557

Stop-and-go kinetics in amyloid fibrillation.

Jesper Ferkinghoff-Borg1, Jesper Fonslet, Christian Beyschau Andersen, Sandeep Krishna, Simone Pigolotti, Hisashi Yagi, Yuji Goto, Daniel Otzen, Mogens H Jensen.   

Abstract

Many human diseases are associated with protein aggregation and fibrillation. We present experiments on in vitro glucagon fibrillation using total internal reflection fluorescence microscopy, providing real-time measurements of single-fibril growth. We find that amyloid fibrils grow in an intermittent fashion, with periods of growth followed by long pauses. The observed exponential distributions of stop and growth times support a Markovian model, in which fibrils shift between the two states with specific rates. Even if the individual rates vary considerably, we observe that the probability of being in the growing (stopping) state is very close to 1/4 (3/4) in all experiments.

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Year:  2010        PMID: 20866557     DOI: 10.1103/PhysRevE.82.010901

Source DB:  PubMed          Journal:  Phys Rev E Stat Nonlin Soft Matter Phys        ISSN: 1539-3755


  17 in total

Review 1.  The nature of amyloid-like glucagon fibrils.

Authors:  Jesper Søndergaard Pedersen
Journal:  J Diabetes Sci Technol       Date:  2010-11-01

2.  An imaging and systems modeling approach to fibril breakage enables prediction of amyloid behavior.

Authors:  Wei-Feng Xue; Sheena E Radford
Journal:  Biophys J       Date:  2013-12-17       Impact factor: 4.033

3.  Polymorph-specific kinetics and thermodynamics of β-amyloid fibril growth.

Authors:  Wei Qiang; Kevin Kelley; Robert Tycko
Journal:  J Am Chem Soc       Date:  2013-04-29       Impact factor: 15.419

4.  High-speed atomic force microscopy reveals structural dynamics of amyloid β1-42 aggregates.

Authors:  Takahiro Watanabe-Nakayama; Kenjiro Ono; Masahiro Itami; Ryoichi Takahashi; David B Teplow; Masahito Yamada
Journal:  Proc Natl Acad Sci U S A       Date:  2016-05-09       Impact factor: 11.205

5.  Frustrated peptide chains at the fibril tip control the kinetics of growth of amyloid-β fibrils.

Authors:  Yuechuan Xu; Kaitlin Knapp; Kyle N Le; Nicholas P Schafer; Mohammad S Safari; Aram Davtyan; Peter G Wolynes; Peter G Vekilov
Journal:  Proc Natl Acad Sci U S A       Date:  2021-09-21       Impact factor: 11.205

6.  Physiological temperature has a crucial role in amyloid β in the absence and presence of hydrophobic and hydrophilic nanoparticles.

Authors:  Mahdi Ghavami; Meisam Rezaei; Reza Ejtehadi; Mina Lotfi; Mohammad A Shokrgozar; Baharak Abd Emamy; Jens Raush; Morteza Mahmoudi
Journal:  ACS Chem Neurosci       Date:  2012-12-14       Impact factor: 4.418

7.  Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states.

Authors:  Laurence J Young; Gabriele S Kaminski Schierle; Clemens F Kaminski
Journal:  Phys Chem Chem Phys       Date:  2017-10-25       Impact factor: 3.945

8.  Inhibitor and substrate cooperate to inhibit amyloid fibril elongation of α-synuclein.

Authors:  Emil Dandanell Agerschou; Vera Borgmann; Michael M Wördehoff; Wolfgang Hoyer
Journal:  Chem Sci       Date:  2020-09-28       Impact factor: 9.825

9.  Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.

Authors:  Dorothea Pinotsi; Alexander K Buell; Celine Galvagnion; Christopher M Dobson; Gabriele S Kaminski Schierle; Clemens F Kaminski
Journal:  Nano Lett       Date:  2013-12-11       Impact factor: 11.189

Review 10.  Misfolding of amyloidogenic proteins and their interactions with membranes.

Authors:  Annalisa Relini; Nadia Marano; Alessandra Gliozzi
Journal:  Biomolecules       Date:  2013-12-27
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