Abstract
Aims: The main aim of this study is to better understand the self-aggregation mechanism of amyloid-like elastin-derived fibers in order to design and produce new powerful drugs that will inhibit the onset of ‘amyloidosis’. Materials & methods: Atomic force microscopy (AFM), Congo Red birefringence assay and Thioflavin T fluorescence measurements were used to demonstrate the amyloid-like behavior of some fragments of elastin protein (exon 30 [EX30] and exon 28 [EX28]). Turbidimetry on apparent absorbance technique was used to investigate the effect either of enhancers or of inhibitors on the amyloidogenic elastin-like peptides. Circular-dichroism spectroscopy was used to study the secondary structures of the peptides. Results & discussion: We used Congo Red birefringence assay, Thioflavin T fluorescence measurements and AFM measurements that are used commonly to demonstrate the formation of amyloids. The elastin fibrillogenesis is amyloid-like. Then, the elastin amyloidogenesis is inhibited by particular pentapeptides. Conclusions: We have reported herein that the fibrillogenesis of elastin-derived EX28 and EX30 polypeptides is facilitated significantly by the effect of sodium taurocholate bile salt and is inhibited by a classical inhibitor of Aβ-amyloid peptide, such as KLVFF, as well as by novel inhibitors, designed by us on the basis of some elastin sequences.
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