0000000000164002

AUTHOR

Kristīne Kitoka

showing 2 related works from this author

High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

2020

AbstractDuring storage in the silk gland, the N-terminal domain (NT) of spider silk proteins (spidroins) keeps the aggregation-prone repetitive region in solution at extreme concentrations. We observe that NTs from different spidroins have co-evolved with their respective repeat region, and now use an NT that is distantly related to previously used NTs, for efficient recombinant production of the amyloid-β peptide (Aβ) implicated in Alzheimer’s disease. A designed variant of NT from Nephila clavipes flagelliform spidroin, which in nature allows production and storage of β-hairpin repeat segments, gives exceptionally high yields of different human Aβ variants as a solubility tag. This tool e…

Models Molecular0301 basic medicineProtein domainBiophysicslcsh:MedicinePeptideBiosynthesis010402 general chemistryBiochemistry01 natural sciencesArticlelaw.invention03 medical and health sciencesProtein DomainslawAnimalsSpider silkAmino Acid SequenceNeurodegenerationlcsh:SciencePeptide sequencechemistry.chemical_classificationAmyloid beta-PeptidesMultidisciplinarybiologySpidroinlcsh:RNeurodegenerative diseasesNephila clavipesProteinsbiology.organism_classification0104 chemical sciences030104 developmental biologyBiochemistrychemistryYield (chemistry)Recombinant DNAlcsh:QPeptidesFibroinsScientific Reports
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Amiloīda-beta 42 peptīda agregācijas pētījumi ar 19F KMR spektroskopiju

2020

Maģistra darba literatūras apskatā apkopota vispārīga informācija par amiloīda-beta peptīdiem, to agregāciju un tās pētīšanas metodēm. Maģistra darbā eksperimentālajā daļā izstrādātas metodes fluorēto aminoskābju inkorporēšanai amiloīda-beta 42 peptīdā, un veikti fluorēto peptīdu KMR eksperimenti.

KMR SPEKTROSKOPIJAAGREGĀCIJAAMILOĪDA-BETAFLUORSAMYLOID-BETAĶīmija
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