| First Author | Chakravarthy B | Year | 2014 |
| Journal | Biochem Biophys Res Commun | Volume | 445 |
| Issue | 3 | Pages | 656-60 |
| PubMed ID | 24569075 | Mgi Jnum | J:219135 |
| Mgi Id | MGI:5619694 | Doi | 10.1016/j.bbrc.2014.02.064 |
| Citation | Chakravarthy B, et al. (2014) Evidence that a synthetic amyloid-ss oligomer-binding peptide (ABP) targets amyloid-ss deposits in transgenic mouse brain and human Alzheimer's disease brain. Biochem Biophys Res Commun 445(3):656-60 |
| abstractText | The synthetic ~5 kDa ABP (amyloid-ss binding peptide) consists of a region of the 228 kDa human pericentrioloar material-1 (PCM-1) protein that selectively and avidly binds in vitro Abeta1-42 oligomers, believed to be key co-drivers of Alzheimer's disease (AD), but not monomers (Chakravarthy et al., (2013) [3]). ABP also prevents Ass1-42 from triggering the apoptotic death of cultured human SHSY5Y neuroblasts, likely by sequestering Ass oligomers, suggesting that it might be a potential AD therapeutic. Here we support this possibility by showing that ABP also recognizes and binds Abeta1-42 aggregates in sections of cortices and hippocampi from brains of AD transgenic mice and human AD patients. More importantly, ABP targets Abeta1-42 aggregates when microinjected into the hippocampi of the brains of live AD transgenic mice. |
