Literature DB >> 30341602

Vesicle-Based Assays to Study Membrane Interactions of Amyloid Peptides.

Ravit Malishev1, Sofiya Kolusheva2, Raz Jelinek3,4.   

Abstract

The growing interest in membrane interactions of amyloidogenic peptides and proteins emanates from the realization that lipid bilayers and membranes play central roles in the toxicity and pathological pathways of amyloid diseases. This chapter presents experimental schemes designed to study membrane interactions and membrane-induced fibrillation of amyloid peptides.

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Keywords:  Amyloid peptides; Amyloid-membrane interactions; Fibrillation; Lipid bilayer fluidity; Membrane dynamics; Membranes

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Year:  2019        PMID: 30341602     DOI: 10.1007/978-1-4939-8820-4_3

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  1 in total

1.  Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes.

Authors:  Maria Ylenia Farrugia; Mario Caruana; Stephanie Ghio; Angelique Camilleri; Claude Farrugia; Ruben J Cauchi; Sara Cappelli; Fabrizio Chiti; Neville Vassallo
Journal:  Sci Rep       Date:  2020-10-20       Impact factor: 4.379

  1 in total

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