Interaction of partially denatured insulin with a DSPC floating lipid bilayer

DOI: 10.1039/C5SM02502H

Authors: A. J. C. Dennison (University Grenoble Alpes) , R. A. L. Jones (The University of Sheffield) , R. A. Staniforth (The University of Sheffield) , A. J. Parnell (The University of Sheffield)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Soft Matter

State: Published (Approved)
Published: November 2015

Abstract: 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.

Subject Areas: Chemistry, Biology and Bio-materials


Instruments: B21-High Throughput SAXS

Added On: 11/12/2015 11:07

Documents:
c5sm02502h.pdf

Discipline Tags:

Non-Communicable Diseases Health & Wellbeing Biochemistry Chemistry Life Sciences & Biotech

Technical Tags:

Scattering Small Angle X-ray Scattering (SAXS)