Identification of Physiological and Toxic Conformations in Aβ42 Aggregates
✍ Scribed by Yuichi Masuda; Satoko Uemura; Ryutaro Ohashi; Azusa Nakanishi; K. Takegoshi; Takahiko Shimizu; Takuji Shirasawa; Kazuhiro Irie
- Book ID
- 102788792
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 641 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1439-4227
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract CD and infrared spectroscopic studies were performed on (i) the inhibitory effects of equimolar quantities of LPFFD‐OH and LPYFD‐NH~2~ on the time‐dependent aggregation of amyloid β‐protein (Aβ) (1–42) and (ii) the β‐sheet‐breaker effects of two‐fold molar excess of the pentapeptides on
## Abstract The amyloid‐β peptide (Aβ) plays a central role in the mechanism of Alzheimer's disease, being the main constituent of the plaque deposits found in AD brains. Aβ amyloid formation and deposition are due to a conformational switching to a β‐enriched secondary structure. Our strategy to i