Inhibiting and Reversing Amyloid‐β Peptide (1–40) Fibril Formation with Gramicidin S and Engineered Analogues

Luo, Jinghui and Otero, Jose M. and Yu, Chien-Hung and Wärmländer, Sebastian K. T. S. and Gräslund, Astrid and Overhand, Mark and Abrahams, Jan Pieter. (2013) Inhibiting and Reversing Amyloid‐β Peptide (1–40) Fibril Formation with Gramicidin S and Engineered Analogues. Chemistry - A European Journal, 19 (51). pp. 17338-17348.

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In Alzheimer's disease, amyloid- (A) peptides aggregate into extracellular fibrillar deposits. Although these deposits may not be the prime cause of the neurodegeneration that characterizes this disease, inhibition or dissolution of amyloid fibril formation by A peptides is likely to affect its development. ThT fluorescence measurements and AFM images showed that the natural antibiotic gramicidinS significantly inhibited A amyloid formation in vitro and could dissolve amyloids that had formed in the absence of the antibiotic. In silico docking suggested that gramicidinS, a cyclic decapeptide that adopts a -sheet conformation, binds to the A peptide hairpin-stacked fibril through -sheet interactions. This may explain why gramicidinS reduces fibril formation. Analogues of gramicidinS were also tested. An analogue with a potency that was four-times higher than that of the natural product was identified.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:06 Nov 2020 08:34
Deposited On:06 Nov 2020 08:34

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