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Fibrillation of transferrin
Claire Booyjzsen1, Charlotte A Scarff, Ben Moreton
1Department of Chemistry, University of Warwick, Coventry, CV4 7AL, UK.
Biochimica Et Biophysica Acta
|November 29, 2011
Summary
Human transferrin protein can form distinct fibrillar deposits, with dimeric forms creating rounded structures and elongated fibers. These structures do not show classical amyloid formation, but their role in neurological disorders is discussed.
Area of Science:
- Biochemistry
- Structural Biology
- Neuroscience
Background:
- Investigated fibrillar deposits of human serum and recombinant transferrin.
- Examined protein behavior on mica and carbon-coated formvar surfaces.
Purpose of the Study:
- Characterize the nature of transferrin fibrillar deposits.
- Explore potential links between transferrin aggregation and neurological diseases.
Main Methods:
- Atomic force microscopy (AFM) for surface imaging.
- Gel permeation chromatography, mass spectrometry, and dynamic light scattering for aggregation analysis.
- Transmission electron microscopy (TEM) for structural visualization.
- Synchrotron radiation-circular dichroism (SRCD) and dye-binding assays for structural changes.
- Ion mobility-mass spectrometry for gas-phase protein shape analysis.
Main Results:
- AFM revealed monolayer films of flattened transferrin on mica, with elongated fibers forming on top.
- Dimeric transferrin formed rounded structures (~250nm) on carbon-coated grids, unlike monomeric transferrin.
- Transferrin fibrils appeared composed of smaller rounded subunits.
- Dye-binding and SRCD indicated no major structural changes or classical beta-sheet amyloid formation during aggregation.
- Ion mobility-mass spectrometry showed minimal shape differences between apo- and holo-transferrin in the gas phase.
Conclusions:
- Transferrin deformation and aggregation may play a role in neurological disorders like Parkinson's and Alzheimer's disease.
- Discusses the implications of transferrin's behavior in the context of iron transport and related disorders.
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