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  • Pore formation by human stefin B in its native and oligomeric states and the consequent amyloid induced toxicity [Elektronski vir]
    Anderluh, Gregor, 1969- ; Žerovnik, Eva
    It is well documented that amyloid forming peptides and proteins interact with membranes and that this correlates with cytotoxicity. To introduce the theme we give a brief description of some ... amyloidogenic proteins and note their similarities with pore forming toxins (PFTs) and cell penetrating peptides. Human stefin B, a member of the family of cystatins, is an amyloidogenic protein in vitro. This review describes our studies of the interaction of stefin B oligomers and prefibrillar aggregates with model membranes leading to pore formation. We have studied the interaction between human stefin B and artificial membranes of various compositions. We also have prepared distinct sizes and morphologies of stefin B prefibrillar states and assessed their toxicity. Furthermore, we have measured electrical currents through pores formed by stefin B prefibrillar oligomers in a planar lipid bilayer setup. We finally discuss the possible functional and pathological significance of such pores formed by human stefin B.
    Source: Frontiers in molecular neuroscience [Elektronski vir]. - ISSN 1662-5099 (Vol. 5, 2012, str. 1-8 (article 85))
    Type of material - e-article
    Publish date - 2012
    Language - english
    COBISS.SI-ID - 5029658
    DOI

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