Interaction of partially denatured insulin with a DSPC floating lipid bilayer

The carefully controlled permeability of cellular membranes to biological molecules is key to life. In degenerative diseases associated with protein misfolding and aggregation, protein molecules or their aggregates are believed to permeate these barriers and threaten membrane integrity. We used neut...

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Bibliographic Details
Published in:Soft matter 2016-01, Vol.12 (3), p.824-829
Main Authors: Dennison, A. J. C, Jones, R. A. L, Staniforth, R. A, Parnell, A. J
Format: Article
Language:English
Subjects:
Animals
Cattle
Cell Membrane Permeability
Cellular
Diseases
Floating structures
Insulin
Insulin - chemistry
Insulin - metabolism
Lipid Bilayers - chemistry
Lipid Bilayers - metabolism
Lipids
Membranes
Partitioning
Phosphatidylcholines - chemistry
Phosphatidylcholines - metabolism
Protein Aggregates
Protein Denaturation
Protein Folding
Proteins
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Summary:The carefully controlled permeability of cellular membranes to biological molecules is key to life. In degenerative diseases associated with protein misfolding and aggregation, protein molecules or their aggregates are believed to permeate these barriers and threaten membrane integrity. We used neutron reflectivity to study the interaction of insulin, a model amyloidogenic protein, with a DSPC floating lipid bilayer. Structural changes consistent with protein partitioning to the membrane interior and adsorption to a gel phase model lipid bilayer were observed under conditions where the native fold of the protein is significantly destabilised. We propose that the perturbation of the membrane by misfolded proteins involves long term occupation of the membrane by these proteins, rather than transient perforation events. Using neutron reflectivity we measure partitioning of destabilised insulin to the membrane interior. These perforation events will adversely affect the cell membrane permeability, which is key to life.
ISSN:1744-683X
1744-6848
DOI:10.1039/c5sm02502h