Blood-Brain Barrier Penetration of an Aβ-Targeted, Arginine-Rich, D-Enantiomeric Peptide

Jiang et al., Biochemica et Biophysica Acta (2016) - PMID: 27423267

Product(s) used in this publication:  Specialty Peptides


The application of small peptides targeting amyloid beta (Aβ) 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 Aβ in different assembly states and eliminate toxic Aβ 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-brainbarrier (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.

Copyright © 2016 Elsevier B.V. All rights reserved.


Alzheimer's disease; Amyloid beta; Arginine-rich motif of HIV-Tat protein; Blood-brainbarrierpenetration; Transgenic mouse models; d-Enantiomericpeptide

Stay in touch and be the first to receive the latest news!