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SAMOORGANIZACIJA TRIPEPTIDNIH HIDROGELATORA KAO MODELA AGREGIRANJA Aβ-PROTEINA


Pospišil, Tihomir; Frkanec, Leo; Žinić, Mladen
SAMOORGANIZACIJA TRIPEPTIDNIH HIDROGELATORA KAO MODELA AGREGIRANJA Aβ-PROTEINA // XXIV. Hrvatski skup kemičara i kemijskih inženjera, Knjiga sažetaka / Š. Ukić ; T. Bolanča (ur.).
Zagreb: Hrvatsko društvo kemijskih inženjera i tehnologa, 2015. str. 171-171 (poster, domaća recenzija, sažetak, ostalo)


Naslov
SAMOORGANIZACIJA TRIPEPTIDNIH HIDROGELATORA KAO MODELA AGREGIRANJA Aβ-PROTEINA
(SELF-ASSEMBLY OF TRIPEPTIDE HYDROGELATORS AS A MODEL OF Aβ-PROTEINS AGGREGATION)

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

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

Izvornik
XXIV. Hrvatski skup kemičara i kemijskih inženjera, Knjiga sažetaka / Š. Ukić ; T. Bolanča - Zagreb : Hrvatsko društvo kemijskih inženjera i tehnologa, 2015, 171-171

ISBN
978-953-6894-54

Skup
XXIV. Hrvatski skup kemičara i kemijskih inženjera

Mjesto i datum
Zagreb, Hrvatska, 21-24.04.2015

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
SAMOORGANIZACIJA TRIPEPTIDNIH HIDROGELATORA
(SELF-ASSEMBLY OF TRIPEPTIDE HYDROGELATORS)

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Projekt / tema
HRZZ-IP-2013-11-7387 - Supramolekulska sinteza samo-organizirajućih funkcionalnih nanomaterijala i kompleksnih kemijskih sustava (Leo Frkanec, )

Ustanove
Institut "Ruđer Bošković", Zagreb