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dc.contributor.authorSun, Xicui
dc.contributor.authorDuan, Songwei
dc.contributor.authorCao, Anna
dc.contributor.authorVillagomez, Bryan
dc.contributor.authorLin, Runxuan
dc.contributor.authorChen, Hongxia
dc.contributor.authorPi, Liya
dc.contributor.authorRen, Bin
dc.contributor.authorChen, Rong
dc.contributor.authorChen, Minjie
dc.contributor.authorYing, Zhekang
dc.contributor.authorFang, Shenyun
dc.contributor.authorCao, Qi
dc.date.accessioned2021-08-12T12:10:02Z
dc.date.available2021-08-12T12:10:02Z
dc.date.issued2021-06-08
dc.identifier.urihttp://hdl.handle.net/10713/16365
dc.description.abstractBackground: Current understanding of amyloid-β protein (Aβ) aggregation and toxicity provides an extensive list of drugs for treating Alzheimer's disease (AD); however, one of the most promising strategies for its treatment has been tri-peptides. Objective: The aim of this study is to examine those tri-peptides, such as Arg-Arg-Try (RRY), which have the potential of Aβ1-42 aggregating inhibition and Aβ clearance. Methods: In the present study, in silico, in vitro, and in vivo studies were integrated for screening tri-peptides binding to Aβ, then evaluating its inhibition of aggregation of Aβ, and finally its rescuing cognitive deficit. Results: In the in silico simulations, molecular docking and molecular dynamics determined that seven top-ranking tri-peptides could bind to Aβ1-42 and form stable complexes. Circular dichroism, ThT assay, and transmission electron microscope indicated the seven tri-peptides might inhibit the aggregation of Aβ1-42 in vitro. In the in vivo studies, Morris water maze, ELISA, and Diolistic staining were used, and data showed that RRY was capable of rescuing the Aβ1-42-induced cognitive deficit, reducing the Aβ1-42 load and increasing the dendritic spines in the transgenic mouse model. Conclusion: Such converging outcomes from three consecutive studies lead us to conclude that RRY is a preferred inhibitor of Aβ1-42 aggregation and treatment for Aβ-induced cognitive deficit.en_US
dc.description.urihttps://doi.org/10.3233/ADR-210012en_US
dc.language.isoenen_US
dc.publisherIOS Pressen_US
dc.relation.ispartofJournal of Alzheimer's Disease Reportsen_US
dc.rights© 2021 – The authors. Published by IOS Press.en_US
dc.subjectAPP/PS1 transgenic miceen_US
dc.subjectAlzheimer’s diseaseen_US
dc.subjectamyloid-βen_US
dc.subjecthigh throughput screeningen_US
dc.subjectsmall peptideen_US
dc.titleRRY Inhibits Amyloid-β Peptide Aggregation and Neurotoxicityen_US
dc.typeArticleen_US
dc.identifier.doi10.3233/ADR-210012
dc.identifier.pmid34368633
dc.source.volume5
dc.source.issue1
dc.source.beginpage479
dc.source.endpage495
dc.source.countryNetherlands


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