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dc.contributor.authorSoudy, Rania-
dc.contributor.authorPatel, Aarti-
dc.contributor.authorFu, Wen-
dc.contributor.authorKaur, Kamaljit-
dc.contributor.authorMacTavish, David-
dc.contributor.authorWestaway, David-
dc.contributor.authorDavey, Rachel A-
dc.contributor.authorZajac, Jeffrey D-
dc.contributor.authorJhamandas, Jack-
dc.identifier.citationAlzheimer's & Dementia (New York, N. Y.) 2017; 3(1): 44-56en_US
dc.description.abstractAmylin receptor serves as a portal for the expression of deleterious effects of amyloid β-protein (Aβ), a key pathologic hallmark of Alzheimer's disease. Previously, we showed that AC253, an amylin receptor antagonist, is neuroprotective against Aβ toxicity in vitro and abrogates Aβ-induced impairment of hippocampal long-term potentiation. Amyloid precursor protein-overexpressing TgCRND8 mice received intracerebroventricularly AC253 for 5 months. New cyclized peptide cAC253 was synthesized and administered intraperitoneally three times a week for 10 weeks in the same mouse model. Cognitive functions were monitored, and pathologic changes were quantified biochemically and immunohistochemically. AC253, when administered intracerebroventricularly, improves spatial memory and learning, increases synaptic integrity, reduces microglial activation without discernible adverse effects in TgCRND8 mice. cAC253 demonstrates superior brain permeability, better proteolytic stability, and enhanced binding affinity to brain amylin receptors after a single intraperitoneal injection. Furthermore, cAC253 administered intraperitoneally also demonstrates improvement in spatial memory in TgCRND8 mice. Amylin receptor is a therapeutic target for Alzheimer's disease and represents a disease-modifying therapy for this condition.en_US
dc.subjectAC253 peptideen_US
dc.subjectAlzheimer's diseaseen_US
dc.subjectAmylin receptoren_US
dc.subjectAmyloid βen_US
dc.subjectBrain penetrationen_US
dc.subjectIn vivo imagingen_US
dc.titleCyclic AC253, a novel amylin receptor antagonist, improves cognitive deficits in a mouse model of Alzheimer's disease.en_US
dc.typeJournal Articleen_US
dc.identifier.journaltitleAlzheimer's & Dementia (New York, N. Y.)en_US
dc.identifier.affiliationCentre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canadaen_US
dc.identifier.affiliationDepartment of Medicine (Neurology), Neuroscience and Mental Health Institute, University of Alberta, Edmonton, Alberta, Canadaen_US
dc.identifier.affiliationFaculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Alberta, Canadaen_US
dc.identifier.affiliationChapman University School of Pharmacy, Irvine, California, USAen_US
dc.identifier.affiliationDepartment of Biochemistry, University of Alberta, Edmonton, Alberta, Canadaen_US
dc.identifier.affiliationFaculty of Pharmacy, Cairo University, Cairo, Egypten_US
dc.identifier.affiliationMedicine (University of Melbourne)en_US
dc.type.austinJournal Article-, Jeffrey D
item.openairetypeJournal Article-
item.fulltextNo Fulltext-
item.grantfulltextnone- (University of Melbourne)-
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