Ethanol Controls the Self-Assembly and Mesoscopic Properties of Human Insulin Amyloid Spherulites

The Journal of Physical Chemistry. B
Valeria VetriVito Foderà

Abstract

Protein self-assembly into amyloid fibrils or highly hierarchical superstructures is closely linked to neurodegenerative pathologies as Alzheimer's and Parkinson's diseases. Moreover, protein assemblies also emerged as building blocks for bioinspired nanostructured materials. In both the above mentioned fields, the main challenge is to control the growth and properties of the final protein structure. This relies on a more fundamental understanding of how interactions between proteins can determine structures and functions of biomolecular aggregates. Here, we identify a striking effect of the hydration of the single human insulin molecule and solvent properties in controlling hydrophobicity/hydrophilicity, structures, and morphologies of a superstructure named spherulite, observed in connection to Alzheimer's disease. Depending on the presence of ethanol, such structures can incorporate fluorescent molecules with different physicochemical features and span a range of mechanical properties and morphologies. A theoretical model providing a thorough comprehension of the experimental data is developed, highlighting a direct connection between the intimate physical protein-protein interactions, the growth, and the properties of the s...Continue Reading

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Citations

Mar 18, 2020·Microscopy Research and Technique·Giuseppe SancataldoValeria Vetri
Nov 5, 2019·Protein and Peptide Letters·Pritha Mandal, Anisur R Molla
Feb 6, 2021·Biophysical Journal·Kevin PounotGiorgio Schirò
Feb 25, 2021·Angewandte Chemie·Shaofei SongMitchell A Winnik
Nov 16, 2019·The Journal of Physical Chemistry. B·Saumyak MukherjeeBiman Bagchi
Jul 15, 2020·The Journal of Physical Chemistry Letters·Kevin PounotTilo Seydel

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