Molecular Characteristics of a Protease-Resistant, Amyloidogenic and Neurotoxic Peptide Homologous to Residues 106-126 of the Prion Protein

Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: Structural clues for prion propagation

“…The major focus of most of these studies was on amino acid residues 106-126. The short synthetic peptide PrP106-126 is indeed amyloidogenic (25)(26)(27) and seems to be neurotoxic (26,30). However, our data show that, when present in the context of a larger, diseaseassociated prion protein variant huPrP145Stop, the sequence 106-126 alone is insufficient to induce protein fibrillization.…”

“…Previous studies have shown that short synthetic peptides corresponding to various segments within the N-terminal part of PrP can also form amyloid fibrils (25)(26)(27)(28)(29). The major focus of most of these studies was on amino acid residues 106-126.…”

“…It was previously shown that a short synthetic peptide corresponding to residues 106-126 of the prion protein aggregates into oligomeric structures with amyloid-like morphology (25)(26)(27). Therefore, it was of interest to compare the latter oligomers with those formed by the much longer and physiologically more relevant (disease-associated) protein huPrP23-144.…”

Structural Properties of Gerstmann-Sträussler-Scheinker Disease Amyloid Protein

“…The selection of the sequences to be modified was based on previous observations that the region spanning residues 106-147 is central to amyloid fibril formation (20). In particular, a peptide comprising residues 106-126 showed high propensity to adopt stable ␤-sheet secondary structure and to assemble into straight, unbranched amyloid fibrils, similar in ultrastructure to those observed in GSS patients (20)(21)(22). Also, a peptide spanning PrP residues 127-147 (PrP-(127-147)) was able to generate amyloidlike fibrils, resembling scrapie-associated fibrils isolated from subjects with transmissible spongiform encephalopathies (20).…”

A novel human antimicrobial factor targets Pseudomonas aeruginosa through its type III secretion system

“…Enzyme treatment was for 3 h followed by heat inactivation of the enzyme at 100 u C for 1 h. After cooling to room temperature, samples were tested for their antimicrobial activity against PA103, as described in the text. peptides have been previously shown to be highly resistant to proteolysis (Timpl et al, 1983;Selvaggini et al, 1993;Beck et al, 2009). …”