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IAPP surface-induced aggregation and corilagin's inhibitory effect.
Shabeena Jegamohan1,2,3, Maziar Jafari1,3, Frédérique Bérubé1,2
1Department of Chemistry, Université du Québec à Montréal, Montréal, Canada. Bourgault.steve@uqam.ca.
Physical Chemistry Chemical Physics : PCCP
|January 12, 2026
Summary
Surface interactions drive protein aggregation, forming fibrils or particles depending on the material. Corilagin polyphenols show varied inhibition of islet amyloid polypeptide (IAPP) surface aggregation.
Area of Science:
- Biochemistry
- Materials Science
- Biophysics
Background:
- Protein assemblies are crucial for physiological functions but can cause disease.
- Surface interactions significantly influence protein structural changes and aggregation.
- Understanding surface-induced protein aggregation is vital for biopathology and biopharmaceutics.
Purpose of the Study:
- To systematically investigate surface-induced aggregation of islet amyloid polypeptide (IAPP).
- To explore the influence of different polymeric surfaces on IAPP fibril formation.
- To examine the inhibitory effect of corilagin on surface-induced IAPP aggregation.
Main Methods:
- Producing IAPP fibrils exclusively through surface induction on mica and various polymer-coated substrates (PEG, pHEMA, PS).
- Characterizing IAPP adsorption and assembly into protofibrils, fibrils, or spherical nanoparticles.
- Evaluating the impact of corilagin on surface-induced IAPP aggregation patterns.
Main Results:
- IAPP formed distinct structures (protofibrils, fibrils, nanoparticles) based on the substrate's surface properties.
- Surface type critically determined the morphology of IAPP aggregates.
- Corilagin demonstrated differential inhibition of surface-induced IAPP aggregation, varying with substrate.
Conclusions:
- Surface properties dictate the pathways of IAPP aggregation.
- Corilagin's inhibitory efficacy against IAPP aggregation is surface-dependent.
- This study provides insights into controlling protein aggregation at interfaces for therapeutic applications.
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