Direct observation of time-resolved polymorphic states in the self-assembly of end-capped heptapeptides
Adamcik, J., Castelletto, V., Bolisetty, S., Hamley, I. W. and Mezzenga, R. (2011) Direct observation of time-resolved polymorphic states in the self-assembly of end-capped heptapeptides. Angewandte Chemie International Edition, 50 (24). pp. 5495-5498. ISSN 1433-7851
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To link to this article DOI: 10.1002/anie.201100807
Amyloid fibrils resulting from uncontrolled peptide aggregation are associated with several neurodegenerative diseases. Their polymorphism depends on a number of factors including pH, ionic strength, electrostatic interactions, hydrophobic interactions, hydrogen bonding, aromatic stacking interactions, and chirality. Understanding the mechanism of amyloid fibril formation can improve strategies towards the prevention of fibrillation processes and enable a wide range of potential applications in nanotemplating and nanotechnology.
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