Naslov
Ac-FFA-NH2 TRIPEPTIDE HYDROGELATOR AS A MODEL OF BINDING SITE OF Aβ-PROTEIN

Autori
Pospišil, Tihomir ; Frkanec, Leo ; Čaplar, Vesna ; Žinić, Mladen

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
MASC 2013, RSC Macrocyclic and Supramolecular Chemistry Meeting / Cronin. Lee ; Forgan, Ross ; Symes, Mark ; Marshall, Stuart - Glasgow : School of Chemistry, University of Glasgow, 2013, P41-P41

Skup
RSC Macrocyclic and Supramolecular Chemistry Meeting

Mjesto i datum
Glasgow, Ujedinjeno Kraljevstvo, 16.12.2013. - 17.12.2013

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
LMWG; Hydrogel; Self-assembly; Thioflavine T; Congo Red

Sažetak
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 30 nm. FTIR and NMR investigation pointed toward the cross-β structure type of hydrogen bonding of the tripeptide in the gel aggregates. Conjugated dyes (Thioflavine T and Congo Red) are commonly used to stain the plaques in histopathological studies. Fluorescence titration of Ac-FFA-NH2 aqueous solution bellow its minimal gelation concentration with Thioflavin T (ThT) showed increase of ThT emission with increased tripetide concentration and formation of the 1:1 complex with significant association constant. Similar results were obtained with other Aβ-binders. These studies are expected to show if such Aβ-inspired hydrogelator aggregates could serve as a minimalist model of the Aβ-KLVFF binding site and possibly reveal its precise interaction with known and new binding molecules.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA