Literature DB >> 29490242

Quantitative Characterization of Metastability and Heterogeneity of Amyloid Aggregates.

Timir Baran Sil1, Bankanidhi Sahoo1, Subhas Chandra Bera1, Kanchan Garai2.   

Abstract

Amyloids are heterogeneous assemblies of extremely stable fibrillar aggregates of proteins. Although biological activities of the amyloids are dependent on its conformation, quantitative evaluation of heterogeneity of amyloids has been difficult. Here we use disaggregation of the amyloids of tetramethylrhodamine-labeled Aβ (TMR-Aβ) to characterize its stability and heterogeneity. Disaggregation of TMR-Aβ amyloids, monitored by fluorescence recovery of TMR, was negligible in native buffer even at low nanomolar concentrations but the kinetics increased exponentially with addition of denaturants such as urea or GdnCl. However, dissolution of TMR-Aβ amyloids is different from what is expected in the case of thermodynamic solubility. For example, the fraction of soluble amyloids is found to be independent of total concentration of the peptide at all concentrations of the denaturants. Additionally, soluble fraction is dependent on growth conditions such as temperature, pH, and aging of the amyloids. Furthermore, amyloids undissolved in a certain concentration of the denaturant do not show any further dissolution after dilution in the same solvent; instead, these require higher concentrations of the denaturant. Taken together, our results indicate that amyloids are a heterogeneous ensemble of metastable states. Furthermore, dissolution of each structurally homogeneous member requires a unique threshold concentration of denaturant. Fraction of soluble amyloids as a function of concentration of denaturants is found to be sigmoidal. The sigmoidal curve becomes progressively steeper with progressive seeding of the amyloids, although the midpoint remains unchanged. Therefore, heterogeneity of the amyloids is a major determinant of the steepness of the sigmoidal curve. The sigmoidal curve can be fit assuming a normal distribution for the population of the amyloids of various kinetic stabilities. We propose that the mean and the standard deviation of the normal distribution provide quantitative estimates of mean kinetic stability and heterogeneity, respectively, of the amyloids in a certain preparation.
Copyright © 2017 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2018        PMID: 29490242      PMCID: PMC5984995          DOI: 10.1016/j.bpj.2017.12.023

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  58 in total

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5.  Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ.

Authors:  Kanchan Garai; Carl Frieden
Journal:  Proc Natl Acad Sci U S A       Date:  2013-02-11       Impact factor: 11.205

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Journal:  Nature       Date:  2016-09-01       Impact factor: 49.962

7.  Nanoscale Heterogeneity of the Molecular Structure of Individual hIAPP Amyloid Fibrils Revealed with Tip-Enhanced Raman Spectroscopy.

Authors:  Corianne C vandenAkker; Tanja Deckert-Gaudig; Michael Schleeger; Krassimir P Velikov; Volker Deckert; Mischa Bonn; Gijsje H Koenderink
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  1 in total

1.  Hsp70 Inhibits Aggregation of IAPP by Binding to the Heterogeneous Prenucleation Oligomers.

Authors:  Neeraja Chilukoti; Timir Baran Sil; Bankanidhi Sahoo; S Deepa; Sreelakshmi Cherakara; Mithun Maddheshiya; Kanchan Garai
Journal:  Biophys J       Date:  2021-01-06       Impact factor: 4.033

  1 in total

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