Pregled bibliografske jedinice broj: 775545
SAMOORGANIZACIJA TRIPEPTIDNIH HIDROGELATORA KAO MODELA AGREGIRANJA Aβ-PROTEINA
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 (HDKI), 2015. str. 171-171 (poster, domaća recenzija, sažetak, ostalo)
CROSBI ID: 775545 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
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 (HDKI), 2015, 171-171
ISBN
978-953-6894-54
Skup
XXIV. Hrvatski skup kemičara i kemijskih inženjera
Mjesto i datum
Zagreb, Hrvatska, 21.04.2015. - 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
Projekti:
HRZZ-IP-2013-11-7387 - Supramolekulska sinteza samo-organizirajućih funkcionalnih nanomaterijala i kompleksnih kemijskih sustava (SInFONIA) (Frkanec, Leo, HRZZ - 2013-11) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb