SELF-ASSEMBLY OF TRIPEPTIDE HYDROGELATORS AS A MODEL OF Aβ-PROTEINS AGGREGATION (CROSBI ID 626883)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | domaća recenzija
Podaci o odgovornosti
Pospišil, Tihomir ; Frkanec, Leo ; Žinić, Mladen
engleski
SELF-ASSEMBLY OF TRIPEPTIDE HYDROGELATORS AS A MODEL OF Aβ-PROTEINS AGGREGATION
Alzheimer's disease is characterized by the extracellular fibrillar deposits of the 39-42 amino acid amyloid-β proteins (Aβ). It was shown that the KLVFF fragment of Aβ-peptide is responsible for the formation of amyloid fibrils. The self-assembly phenomena of the low molecular weight peptides into supramolecular gels show resemblance to amyloid-β protein aggregation and hence may serve as a simple model for Aβ-aggregation which could enable design of new aggregation inhibitors. We have synthesized a series of new tripeptide gelators incorporating amino acids present in the Aβ- protein KLVFF fragment denoted responsible for the protein aggregation. Prepared peptides were tested for gelation of water and organic solvents. Organisation in gel assemblies at the supramolecular level and gel morphology was determined by using spectroscopic methods (1HNMR, FTIR) and electronic microscopy (TEM). Tripeptide derivative (Ac-FFA-NH2) was capable to self- assemby into hydrogel at physiological pH. Figure 1 shows possible antiparallel β- sheet hydrogen-bonding motifs of Ac-FFA-NH2 in the hydrogel. The aggregated tripeptide binds with conjugated dyes – Thioflavin T and Congo Red representing common reagents for determining specific amyloid fibrillation.
SELF-ASSEMBLY OF TRIPEPTIDE HYDROGELATORS
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Podaci o prilogu
171-171.
2015.
objavljeno
Podaci o matičnoj publikaciji
XXIV. Hrvatski skup kemičara i kemijskih inženjera, Knjiga sažetaka
Š. Ukić ; T. Bolanča
Zagreb: Hrvatsko društvo kemijskih inženjera i tehnologa (HDKI)
978-953-6894-54
Podaci o skupu
XXIV. hrvatski skup kemičara i kemijskih inženjera
poster
21.04.2015-24.04.2015
Zagreb, Hrvatska