Abstract
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.
Highlights
In most neurodegenerative diseases, including Alzheimer’s disease (AD), Parkinson’s disease (PD), frontotemporal dementia, motor neuron disease, and transmissible spongiform encephalopathy (TSE), the specific disease-related protein misfolds into an alternative conformation that tends to form β-sheet rich oligomers and, eventually, amyloid fibrils
This review describes our studies of the interaction of stefin B oligomers and prefibrillar aggregates with model membranes leading to pore formation
Amyloid forming proteins have a strong tendency to interact with lipid membranes and to make pores
Summary
In most neurodegenerative diseases, including Alzheimer’s disease (AD), Parkinson’s disease (PD), frontotemporal dementia, motor neuron disease, and transmissible spongiform encephalopathy (TSE), the specific disease-related protein misfolds into an alternative conformation that tends to form β-sheet rich oligomers and, eventually, amyloid fibrils. This review describes our studies of the interaction of stefin B oligomers and prefibrillar aggregates with model membranes leading to pore formation. In this review we describe membrane interactions and pore formation induced by human stefin B, some of its mutants and different oligomeric states.
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