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Amyloid-Like Aggregates Formation by Bovine Apo-Carbonic Anhydrase in Various Alcohols: A Comparative Study Publisher Pubmed



Eshaghi A1 ; Ebrahimhabibi A2 ; Sabbaghian M3 ; Nematgorgani M4
Authors
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Authors Affiliations
  1. 1. Department of Biology, Mashhad Branch, Islamic Azad University, Mashhad, Iran
  2. 2. Biosensor Research Center, Endocrinology and Metabolism Molecular-Cellular Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran
  3. 3. Department of Andrology at Reproductive Biomedicine Research Center Royan Institute for Reproductive Biomedicine, ACECR, Tehran, Iran
  4. 4. Stanford Genome Technology Center, Stanford University, Palo Alto, CA, United States

Source: International Journal of Biological Macromolecules Published:2016


Abstract

Peptides and proteins convert from their native states to amyloid fibrillar aggregates in a number of pathological conditions. Characterizing these species could provide useful information on their pathogenicity and the key factors involved in their generation. In this study, we have observed the ability of the model protein apo-bovine carbonic anhydrase (apo-BCA) to form amyloid-like aggregates in the presence of halogenated and non-halogenated alcohols. Far-UV circular dichroism, ThT fluorescence, atomic force microscopy and dynamic light scattering were used to characterize these structures. The concentration required for effective protein aggregation varied between the solvents, with non-halogenated alcohols acting in a wider range. These aggregates show amyloid-like structures as determined by specific techniques used for characterizing amyloid structures. Oligomers were obtained with various size distributions, but fibrillar structures were not observed. Use of halogenated alcohols resulted into smaller hydrodynamic radii, and most stable oligomers were formed in hexafluoropropan-2-ol (HFIP). At optimal concentrations used to generate these structures, the non-halogenated alcohols showed higher hydrophobicity, which may be related to the lower stability of the generated oligomers. These oligomers have the potential to be used as models in the search for effective treatments in proteinopathies. © 2016 Elsevier B.V.