Amyloid Fiber Formation by Synthetic Peptides Derived from the Sequence of the Protein CsgA of Escherichia coli

Title:Amyloid Fiber Formation by Synthetic Peptides Derived from the Sequence of the Protein CsgA of Escherichia coli

Volume: 20 Issue: 8

Author(s): Pierre Lembre, Charlotte Vendrely and Patrick Di Martino

Affiliation:

Keywords: Amyloïd, biofilm, CsgA, Curli, fiber, peptide.

Abstract: We characterized the formation of amyloid fibers by two peptides derived from the CsgA sequence: R5 (133- 151) corresponding to the whole repeating unit R5 and a truncated form of this peptide called R5T (134-143). In the presence of either of the two peptides: an increase in the fluorescence intensity of Thioflavin T was observed; a shift of the absorbance of Congo red was measured; spontaneous formation of amyloid fibers was observed by polarized light as well asatomic force microscopy imaging. Large-size aggregates were observed with R5 while R5T formed fagots of individualized fibers. The infrared spectroscopy analysis revealed the presence of a greater number of intermolecular bonds for R5. In conclusion, a 10 aminoacids peptide derived from the R5 sequence was sufficient for the spontaneous formation of amyloid fibrils but not to form large-size aggregates of fibers.

Cite this article as:

Lembre Pierre, Vendrely Charlotte and Martino Di Patrick, Amyloid Fiber Formation by Synthetic Peptides Derived from the Sequence of the Protein CsgA of Escherichia coli, Protein & Peptide Letters 2013; 20 (8) . https://dx.doi.org/10.2174/0929866511320080012