NR AWDF
AU Chang,E.S.H.; Chen,R.P.Y.
TI Studying the sequence dependent amyloid fibril formation
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions S-05
PT Konferenz-Poster
AB The common characteristic of Prion disease and Alzheimer's disease is the formation of amyloid plaque in brain. Amyloid is a special structural form composed of cross ß-sheet structure. Compared with the prion protein, the major components of the amyloid in Alzheimer's disease, Aß40 and Aß42 peptides, is much more prone to aggregate into the amyloid. Here, we use Aß40 peptide as our studying system and try to explore how sequence determines the amyloid formation and why the polypeptide chain tends to associate into amyloid fibril rather than other ß-sheet structures. The D.form proline (DP) has been widely used in designed peptide as the DP-G sequence tends to form a type II' ß-turn which is the favorite turn type in the formation of ß-hairpin. We substituted each amino acid residue in front of the Gly residue of the Aß40 peptide to D-form proline individually to create five peptides containing the DP-G sequence at different positions. The ß-structure formation of these peptides was monitored by the Circular Dichroism (CD) spectroscopy. The amyloidogenesis was affected by these mutations differently. Interestingly, we found the V24P mutation could reversibly form a ß-sheet-rich species, depending on the peptide concentration. And the structure also shows Thioflavin-T and Congo-Red binding ability.
AD Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, ROC. E-mail: pyc@gate.sinica.edu.tw
SP englisch
PO Italien