Abstract
Two tetrapeptides, HAEE and RADD, which are ionic-complementary to the primary zinc recognition site of amyloid-β (Aβ), have been reported to inhibit zinc-induced dimerization of the Aβ metal-binding domain and slow Aβ aggregation in vitro. In the present study, we investigate the impact of HAEE and RADD on the development of cerebral β-amyloidosis in a mouse model of Alzheimer's disease. We have found chronic intravenous administration of each peptide results in significant decrease of amyloid plaque burden in the treated mice.
Keywords:
Alzheimer’s disease; amyloid-β; mouse models; protein aggregation in vivo.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Alzheimer Disease / drug therapy*
-
Alzheimer Disease / pathology*
-
Amyloid beta-Peptides / chemistry*
-
Amyloid beta-Protein Precursor / genetics
-
Animals
-
Antipsychotic Agents / therapeutic use*
-
Brain / drug effects
-
Brain / metabolism
-
Brain / pathology
-
Disease Models, Animal
-
Humans
-
Injections, Intravenous
-
Mice
-
Mice, Inbred C57BL
-
Mice, Transgenic
-
Mutation / genetics
-
Oligopeptides / therapeutic use*
-
Plaque, Amyloid / drug therapy
-
Plaque, Amyloid / genetics
-
Presenilin-1 / genetics
Substances
-
Amyloid beta-Peptides
-
Amyloid beta-Protein Precursor
-
Antipsychotic Agents
-
Oligopeptides
-
Presenilin-1