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A new fibrillization mechanism of ß-lactoglobulin in glycine solutions
ID
Jaklin, Matej
(
Avtor
),
ID
Hritz, Jozef
(
Avtor
),
ID
Hribar-Lee, Barbara
(
Avtor
)
PDF - Predstavitvena datoteka,
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(5,42 MB)
MD5: 2B3DCAB209B229AF79D73B9A76246216
URL - Izvorni URL, za dostop obiščite
https://www.sciencedirect.com/science/article/pii/S0141813022013952
Galerija slik
Izvleček
Even though amyloid aggregates were discovered many years ago the mechanism of their formation is still a mystery. Because of their connection to many of untreatable neurodegenerative diseases the motivation for finding a common aggregation path is high. We report a new high heat induced fibrillization path of a model protein β-lactoglobulin (BLG) when incubated in glycine instead of water at pH 2. By combining atomic force microscopy (AFM), transmission emission microscopy (TEM), dynamic light scattering (DLS) and circular dichroism (CD) we predict that the basic building blocks of fibrils made in glycine are not peptides, but rather spheroid oligomers of different height that form by stacking of ring-like structures. Spheroid oligomers linearly align to form fibrils by opening up and combining. We suspect that glycine acts as an hydrolysation inhibitor which consequently promotes a different fibrillization path. By combining the known data on fibrillization in water with our experimental conclusions we come up with a new fibrillization scheme for BLG. We show that by changing the fibrillization conditions just by small changes in buffer composition can dramatically change the aggregation pathway and the effect of buffer shouldn't be neglected. Fibrils seen in our study are also gaining more and more attention because of their pore-like structure and a possible cytotoxic mechanism by forming pernicious ion-channels. By preparing them in a simple model system as BLG we opened a new way to study their formation.
Jezik:
Angleški jezik
Ključne besede:
ß-lactoglobulin
,
fibrillization mechanism
,
buffer specific effects
,
spheroid oligomers
Vrsta gradiva:
Članek v reviji
Tipologija:
1.01 - Izvirni znanstveni članek
Organizacija:
FKKT - Fakulteta za kemijo in kemijsko tehnologijo
Status publikacije:
Objavljeno
Različica publikacije:
Objavljena publikacija
Leto izida:
2022
Št. strani:
Str. 414-425
Številčenje:
Vol. 216
PID:
20.500.12556/RUL-138811
UDK:
577.322
ISSN pri članku:
0141-8130
DOI:
10.1016/j.ijbiomac.2022.06.182
COBISS.SI-ID:
114740483
Datum objave v RUL:
19.08.2022
Število ogledov:
511
Število prenosov:
130
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Objavi na:
Gradivo je del revije
Naslov:
International journal of biological macromolecules
Skrajšan naslov:
Int. j. biol. macromol.
Založnik:
Elsevier
ISSN:
0141-8130
COBISS.SI-ID:
25637888
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
Opis:
Najbolj omejujoča licenca Creative Commons. Uporabniki lahko prenesejo in delijo delo v nekomercialne namene in ga ne smejo uporabiti za nobene druge namene.
Sekundarni jezik
Jezik:
Slovenski jezik
Ključne besede:
ß-laktoglobulin
,
fibrilizacijski mehanizem
,
pufer specifični efekt
,
sferoidni oligomeri
Projekti
Financer:
NIH - National Institutes of Health
Številka projekta:
RM1GM135136
Financer:
Drugi - Drug financer ali več financerjev
Program financ.:
Czech Science Foundation
Številka projekta:
GF20-05789L
Financer:
Drugi - Drug financer ali več financerjev
Program financ.:
MEYS CR, Instruct-CZ Centre, CIISB
Številka projekta:
LM201812
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