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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

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Sterol Structure Strongly Modulates Membrane-Islet Amyloid Polypeptide Interactions.

Xiaoxue Zhang, Erwin London, Daniel P Raleigh

|January 27, 2018

Summary

Sterols influence amyloid formation by altering membrane order, impacting human islet amyloid polypeptide (IAPP) binding and cytotoxicity in type-2 diabetes research. Specific sterol-IAPP interactions play a minor role.

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Amyloid formation is linked to various human diseases.
Human islet amyloid polypeptide (IAPP) aggregation contributes to type-2 diabetes pathology.
IAPP-membrane interactions are critical for cytotoxicity and disease progression.

Purpose of the Study:

To investigate the role of sterols in IAPP-membrane interactions.
To determine if sterol effects are due to general membrane properties or specific IAPP-sterol interactions.
To examine how different sterols modulate IAPP binding, membrane disruption, and amyloid formation.

Main Methods:

Utilized model membranes with varying sterol compositions.
Measured IAPP binding to membranes using fluorescence anisotropy.
Assessed membrane disruption via leakage assays.
Quantified amyloid formation kinetics.

Main Results:

Sterol effects on IAPP-membrane interactions primarily correlated with their impact on membrane order.
Specific IAPP-sterol interactions had minimal influence.
Reduced IAPP binding and membrane leakage were observed with increased membrane order.
Amyloid formation time was inversely related to sterol-induced membrane order.

Conclusions:

Membrane order, modulated by sterols, is the dominant factor in IAPP-membrane interactions.
The binding of IAPP to a specific subset of vesicles, influenced by membrane order, dictates cytotoxicity.
Findings provide insights into the mechanisms of IAPP-mediated cell death in type-2 diabetes.