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Naslov:The effect of three polyphenols and some other anti-oxidant substances on amyloid fibril formation by human cystatin C
Avtorji:ID Jahić, Alma (Avtor)
ID Tušek-Žnidarič, Magda (Avtor)
ID Pintar, Sara (Avtor)
ID Berbić, Selma (Avtor)
ID Žerovnik, Eva (Avtor)
Datoteke:URL URL - Izvorni URL, za dostop obiščite http://dx.doi.org/10.1016/j.neuint.2020.104806
 
.pdf PDF - Predstavitvena datoteka, prenos (7,93 MB)
MD5: AE8CB27FCAB7F417731B068312F84F37
 
Jezik:Angleški jezik
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:Logo NIB - Nacionalni inštitut za biologijo
Povzetek:Human cystatin C (CysC) is an amyloid forming protein involved in the hereditary cerebral amyloid angiopathy (HCCAA) that affects arteries in the brain and the peripheral nervous system. In this study we measured the influence of several substances on human CysC aggregation and amyloid fibril formation, induced at pH 4 in vitro. The effect of three polyphenols: resveratrol, quercetin and curcumin and of two antioxidants: vitamin C (VitC) and N-acetyl-L-cysteine (NAC) was explored as well as the effect of sulphoraphane (SF) and α-lipoic acid (AL). The formation of amyloid fibrils was followed by Thioflavin T (ThT) fluorescence and by transmission electron microscopy (TEM). Effects on the length of the lag phase were revealed by following the increase of ThT fluorescence intensity with time. The amount and morphology of fibrils in comparison to prefibrillar aggregates and globular oligomers were evaluated by TEM at the plateau stage of the reaction. Thermal stabilization of the CysC monomer by the small compounds was measured by differential scanning fluorimetry (DSF). NAC, VitC and SF exhibited the largest inhibitory effect on amyloid fibril growth. The effects of polyphenols were not significant, apart from resveratrol, which partly inhibited the amyloid fibril growth.
Verzija publikacije:Objavljena publikacija
Datum objave:01.11.2020
Leto izida:2020
Št. strani:str. 1-9
Številčenje:Vol. 140
PID:20.500.12556/DiRROS-19524 Novo okno
UDK:577
ISSN pri članku:0197-0186
DOI:10.1016/j.neuint.2020.104806 Novo okno
COBISS.SI-ID:26233859 Novo okno
Datum objave v DiRROS:22.07.2024
Število ogledov:8
Število prenosov:3
Metapodatki:XML RDF-CHPDL DC-XML DC-RDF
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Gradivo je del revije

Naslov:Neurochemistry International
Skrajšan naslov:Neurochem. int.
Založnik:Pergamon Press
ISSN:0197-0186
COBISS.SI-ID:26012928 Novo okno

Gradivo je financirano iz projekta

Financer:ARIS - Javna agencija za znanstvenoraziskovalno in inovacijsko dejavnost Republike Slovenije
Številka projekta:P1-0140-2015
Naslov:Proteoliza in njena regulacija

Licence

Licenca:CC BY-NC-ND 4.0, Creative Commons Priznanje avtorstva-Nekomercialno-Brez predelav 4.0 Mednarodna
Povezava:http://creativecommons.org/licenses/by-nc-nd/4.0/deed.sl
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