Reversible Assembly of a Drug Peptide into Amyloid Fibrils: A Dynamic Circular Dichroism Study

Langmuir : the ACS Journal of Surfaces and Colloids
Frédéric Gobeaux, Frank Wien

Abstract

The common view on the amyloid fibril formation is that it is a multistep process that involves many oligomeric intermediate species, which leads to a high degree of polymorphism. This view derives from numerous kinetic studies whose vast majority was carried out with amyloid β fragments or other pathological amyloidogenic sequences. Yet, it is not clear whether the mechanisms inferred from these studies are universal and also apply to functional amyloids, in particular to peptide hormones which form reversible amyloid structures. In the present work, we study the self-assembly properties of atosiban, a nonapeptide drug, whose sequence is very close to those of the oxytocin and vasopressin hormones. We show that this very soluble peptide consistently self-assembles into 7 nm wide amyloid fibrils above a critical aggregation concentration (2-10 w/w % depending on the buffer conditions). The peptide system is characterized in details, from the monomeric to the assembled form, with osmotic concentration measurements, transmission electron microscopy, small-angle X-ray scattering, infrared and fluorescence spectroscopy, and circular dichroism (CD). We have followed in situ the fibril assembly with fluorescence and synchrotron radia...Continue Reading

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Citations

Nov 16, 2018·Scientific Reports·Antoine MalabiradeVéronique Arluison
Jan 26, 2021·Journal of Peptide Science : an Official Publication of the European Peptide Society·Carlo DiaferiaGiancarlo Morelli
Jun 8, 2021·Bioorganic Chemistry·Daniele FlorioDaniela Marasco
Dec 5, 2021·The FEBS Journal·Joëlle A J HousmansFrederic Rousseau

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