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Nanoparticles modulate membrane interactions of human Islet amyloid polypeptide (hIAPP)
Yossef Peretz1, Ravit Malishev1, Sofiya Kolusheva2
1Department of Chemistry, Ben Gurion University of the Negev, Beer Sheva 84105, Israel.
Biochimica Et Biophysica Acta. Biomembranes
|April 12, 2018
Summary
Nanoparticles (NPs) did not alter human islet amyloid polypeptide (hIAPP) fibrillation but enhanced its interactions with cell membranes. This suggests potential toxicity risks when NPs and amyloidogenic peptides coexist.
Area of Science:
- Nanotechnology
- Biochemistry
- Materials Science
Background:
- Nanomaterials and nanoparticles (NPs) are increasingly used in consumer products.
- Potential health risks associated with NP exposure are a growing concern.
- Human islet amyloid polypeptide (hIAPP) aggregation is linked to type 2 diabetes.
Purpose of the Study:
- To investigate the impact of various NPs on hIAPP fibrillation and membrane interactions.
- To assess how NP composition and surface properties affect these processes.
- To explore potential toxicity and pathogenicity risks.
Main Methods:
- Co-incubation of hIAPP with different NPs (polymeric, TiO2, Au NPs) in buffer and biomimetic vesicle solutions.
- Spectroscopic and microscopic analyses to study fibrillation and morphology.
- Evaluation of NP-hIAPP synergistic bilayer interactions.
Main Results:
- NPs did not significantly interfere with hIAPP fibrillation or fibril morphology.
- NPs appeared to promote membrane-induced hIAPP fibrillation.
- All examined NPs showed more pronounced, synergistic bilayer interactions with hIAPP.
- NP-enhanced interactions were independent of NP composition and surface properties.
Conclusions:
- Nanoparticles do not inhibit but may promote hIAPP fibrillation.
- Co-incubation of NPs with hIAPP leads to significantly enhanced bilayer interactions.
- These NP-hIAPP interactions may indicate potential toxicity and pathogenicity risks.
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