The anti-amyloidogenic activity in the chaperone DNAJB6 and mimic constructs with only the most conserved serine and threonine rich beta-hairpin
Proteiner som hjälper andra proteiner att bevara deras struktur genom att binda in till dem kallas chaperoner. Chaperonet DNAJB6 (se figur nedan) finns bland annat i människokroppen och hjälper till att hindra vissa aggregeringsbenägna peptider, som amyloid-β, från att aggregera till fibriller. Fibriller av amyloid-β är kopplade till neurodegenerativa sjukdomar så som Huntington och Alzheimer. I fThe chaperone DNAJB6 can suppress fibril formation of amyloid-β. This is dependent on functionally important conserved serine (S) and threonine (T) residues located in a C-terminal domain which is dominated by β-strands. Substitution of the conserved ST-residues with alanine residues results in loss of this function. In this thesis two DNAJB6 mimic constructs are examined to see whether or not the