NPT088 reduces both amyloid-β and tau pathologies in transgenic mice.

ABSTRACT: INTRODUCTION:Alzheimer's disease (AD) is characterized by appearance of both extracellular senile plaques and intracellular neurofibrillary tangles, comprised of aggregates of misfolded amyloid-β (Aβ) and hyper-phosphorylated tau, respectively. In a previous study, we demonstrated that g3p, a capsid protein from bacteriophage M13, binds to and remodels misfolded aggregates of proteins that assume an amyloid conformation. We engineered a fusion protein ("NPT088") consisting of the active fragment of g3p and human-IgG1-Fc. METHODS:Aged Tg2576 mice or rTg4510 mice received NPT088 weekly via IP injection. Cognitive and/or functional motor endpoints were monitored during dosing. Pathology was quantified biochemically and immunohistochemically. RESULTS:NPT088-lowered Aβ plaque and improved cogni

SUBMITTER: Levenson JM 

PROVIDER: S-EPMC5651359 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature