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- W3044634796 abstract "Abstract One of the main culprits of Alzheimer’s disease (AD) is the formation of toxic amyloid-β (Aβ) peptide polymers and the aggregation of Aβ to form plaques in the brain. We have developed techniques to purify the catalytic domain of plasmin, micro-plasmin (µPlm), which can be used for an Aβ-clearance based AD therapy. However, in serum, µPlm is irreversibly inhibited by its principal inhibitor α2-antiplasmin (α2-AP). In this study, we engineered and selected mutant forms of µPlm that are both catalytically active and insensitive to α2-AP inhibition. We identified surface residues of μPlm that might interact and bind α2-AP, and used an alanine-scanning mutagenesis method to select residues having higher activity but lower α2-AP inhibition. Then we employed saturation mutagenesis for further optimize both properties. Modeled complex structure of µPlm/α2-AP shows that F587 is a critical contact residue, which can be used as a starting position for further investigation." @default.
- W3044634796 created "2020-07-29" @default.
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- W3044634796 date "2020-07-21" @default.
- W3044634796 modified "2023-10-06" @default.
- W3044634796 title "Selection of mutant µplasmin for amyloid-β cleavage in vivo" @default.
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- W3044634796 doi "https://doi.org/10.1038/s41598-020-69079-8" @default.
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