engleski

Tripeptide hydrogelator (Ac-FFA-NH2) as a model of binding site Aβ-protein ; comparative binding studies with Thioflavin-T and other Aβ- binders

Series of tripeptide FFA derivatives was synthesized and tested for gelation of water and organic solvents. Only Ac-FFA-NH2 tripeptide exhibited gelation of water by self- assembly under physiological conditions. TEM of the Ac- FFA-NH2 hydrogel and the methanol/water gel showed the presence of straight fibers with relatively uniform diameters of around 50 nm. FTIR and NMR investigation pointed toward the cross-β structure type of hydrogen bonding of the tripeptide in the gel aggregates. Conjugated dyes (Thioflavin T and Congo Red) are commonly used to stain the plaques in histopathological studies3. Fluorescence titration of Ac-FFA-NH2 aqueous solution bellow its minimal gelation concentration with Thioflavin T (ThT) showed increase of ThT emission with increased tripeptide concentration and formation of the 1 : 1 complex with significant association constant.

Aβ-amyloid aggregates; Supramolecular self assembly; Low molecular weight peptidic gelators; Binding of histological dyes

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