English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

We identified that JAL-TA9, a 9-mer synthetic peptide derived from Tob1 protein, possesses catalytic activity and cleaves Aβ42. We also determined that the C-terminal end of Prion protein (PrP) is an essential region for aggregation of PrP using PrP fragment peptides. We investigated the effect of JAL-TA9 on hPrP180-192, which is a fragment peptide derived from human prion protein. Conformational studies were performed using CD analysis. The cleavage reaction was identified using HPLC and MS analyses. JAL TA9 inhibited the formation of aggregated hPrP180-192 and decreased the aggregated hPrP180-192 level through the cleavage reaction. These results indicate that JAL-TA9 could be a promising candidate for developing novel drugs against prion diseases and Alzheimer’s disease.

JAL-TA9 Inhibits Aggregation of Hprp180-192 through the Cleavage Reaction