Biofilm associated proteins (Bap) are involved in the biofilm formation process of several bacterial species.
The sequence STVTVT is present in Bap proteins expressed by many Staphylococcus species, Acinetobacter
baumanii and Salmonella enterica. The peptide STVTVTF derived from the C-repeat of the Bap protein from
Staphylococcus epidermidis was selected through the AGGRESCAN, PASTA, and TANGO software prediction of protein
aggregation and formation of amyloid fibers. We characterized the self-assembly properties of the peptide
STVTVTF by different methods: in the presence of the peptide, we observed an increase in the fluorescence intensity
of Thioflavin T; many intermolecular β-sheets and fibers were spontaneously formed in peptide preparations
as observed by infrared spectroscopy and atomic force microscopy analyses. In conclusion, a 7 amino acids peptide
derived from the C-repeat of the Bap protein was sufficient for the spontaneous formation of amyloid fibers.
The possible involvement of this amyloidogenic sequence in protein-protein interactions is discussed.
Keywords: Amyloid, bap, biofilm, peptide, Staphylococcus epidermidis.
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