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Pregled bibliografske jedinice broj: 675168

Zbornik radova

Autori: Pospišil, Tihomir; Frkanec, Leo; Čaplar, Vesna; Žinić, Mladen
Naslov: Ac-FFA-NH2 TRIPEPTIDE HYDROGELATOR AS A MODEL OF BINDING SITE OF Aβ-PROTEIN
Izvornik: MASC 2013, RSC Macrocyclic and Supramolecular Chemistry Meeting / Cronin. Lee ; Forgan, Ross ; Symes, Mark ; Marshall, Stuart (ur.). - Glasgow : School of Chemistry, University of Glasgow , 2013. P41-P41.
Skup: RSC Macrocyclic and Supramolecular Chemistry Meeting
Mjesto i datum: Glasgow, UK, 16-17. 12. 2013.
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.
Vrsta sudjelovanja: Poster
Vrsta prezentacije u zborniku: Sažetak
Vrsta recenzije: Međunarodna recenzija
Izvorni jezik: ENG
Kategorija: Znanstveni
Znanstvena područja:
Kemija
Upisao u CROSBI: Leo Frkanec (Leo.Frkanec@irb.hr), 8. Sij. 2014. u 10:03 sati



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