| First Author | Jiang N | Year | 2016 |
| Journal | Biochim Biophys Acta | Volume | 1858 |
| Issue | 11 | Pages | 2717-2724 |
| PubMed ID | 27423267 | Mgi Jnum | J:255419 |
| Mgi Id | MGI:6105042 | Doi | 10.1016/j.bbamem.2016.07.002 |
| Citation | Jiang N, et al. (2016) Blood-brain barrier penetration of an Abeta-targeted, arginine-rich, d-enantiomeric peptide. Biochim Biophys Acta 1858(11):2717-2724 |
| abstractText | The application of small peptides targeting amyloid beta (Abeta) is one of many drug development strategies for the treatment of Alzheimer''s disease (AD). We have previously identified several peptides consisting solely of D-enantiomeric amino acid residues obtained from mirror-image phage display selection, which bind to Abeta in different assembly states and eliminate toxic Abeta aggregates. Some of these D-peptides show both diagnostic and therapeutic potential in vitro and in vivo. Here we have analysed the similarity of the arginine-rich D-peptide D3 to the arginine-rich motif (ARM) of the human immunodeficiency virus type 1 transactivator of transcription (HIV-Tat) protein, and examined its in vivo blood-brain barrier (BBB) permeability using wild type mice and transgenic mouse models of Alzheimer''s disease. We are able to demonstrate that D3 rapidly enters the brain where it can be found associated with amyloid plaques suggesting a direct penetration of BBB. |
