Amyloid-like properties of a synthetic peptide corresponding to the carboxy terminus of β-amyloid protein precursor
| Autor: | Daniel A. Kirschner, Claudia B. Caputo, Paul E. Fraser, Irene R. Evangelista Sobel |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Protein Conformation
Swine Stereochemistry Molecular Sequence Data Biophysics Peptide Biochemistry Amyloid beta-Protein Precursor Structure-Activity Relationship chemistry.chemical_compound Protein structure X-Ray Diffraction Endopeptidases mental disorders Amyloid precursor protein Animals Amino Acid Sequence Protein precursor Molecular Biology Peptide sequence chemistry.chemical_classification Serum Amyloid A Protein biology Hydrolysis Amino acid Congo red chemistry biology.protein Thioflavin Peptides |
| Zdroj: | Archives of Biochemistry and Biophysics. 292:199-205 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(92)90068-8 |
| Popis: | A synthetic peptide whose sequence corresponds to the 20 carboxy-terminal amino acids of beta-amyloid protein precursor (APP) was found to form fibrils in vitro. These fibrils showed birefringence in polarized light when stained with Congo red, fluoresced when bound with thioflavin S, were resistant to proteases, and had a cross-beta conformation. By contrast, peptides with other sequences from the intracellular domain of APP and a peptide corresponding to this entire domain did not exhibit the full range of beta-amyloid properties. These results suggest that a fragment from the C-terminus of the beta-amyloid protein precursor could bind to intraneuronal paired helical filaments and account for some of its amyloid-like properties. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|