Ac-FFA-NH2 TRIPEPTIDE HYDROGELATOR AS A MODEL OF BINDING SITE OF Aβ-PROTEIN (CROSBI ID 606554)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Pospišil, Tihomir ; Frkanec, Leo ; Čaplar, Vesna ; Žinić, Mladen
engleski
Ac-FFA-NH2 TRIPEPTIDE HYDROGELATOR AS A MODEL OF BINDING SITE OF Aβ-PROTEIN
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.
LMWG; Hydrogel; Self-assembly; Thioflavine T; Congo Red
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Podaci o prilogu
P41-P41.
2013.
objavljeno
Podaci o matičnoj publikaciji
MASC 2013, RSC Macrocyclic and Supramolecular Chemistry Meeting
Cronin. Lee ; Forgan, Ross ; Symes, Mark ; Marshall, Stuart
Glasgow: School of Chemistry, University of Glasgow
Podaci o skupu
RSC Macrocyclic and Supramolecular Chemistry Meeting
poster
16.12.2013-17.12.2013
Glasgow, Ujedinjeno Kraljevstvo