Your browser does not allow JavaScript!
JavaScript is necessary for the proper functioning of this website. Please enable JavaScript or use a modern browser.
Open Science Slovenia
Open Science
DiKUL
slv
|
eng
Search
Browse
New in RUL
About RUL
In numbers
Help
Sign in
A new fibrillization mechanism of ß-lactoglobulin in glycine solutions
ID
Jaklin, Matej
(
Author
),
ID
Hritz, Jozef
(
Author
),
ID
Hribar-Lee, Barbara
(
Author
)
PDF - Presentation file,
Download
(5,42 MB)
MD5: 2B3DCAB209B229AF79D73B9A76246216
URL - Source URL, Visit
https://www.sciencedirect.com/science/article/pii/S0141813022013952
Image galllery
Abstract
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.
Language:
English
Keywords:
ß-lactoglobulin
,
fibrillization mechanism
,
buffer specific effects
,
spheroid oligomers
Work type:
Article
Typology:
1.01 - Original Scientific Article
Organization:
FKKT - Faculty of Chemistry and Chemical Technology
Publication status:
Published
Publication version:
Version of Record
Year:
2022
Number of pages:
Str. 414-425
Numbering:
Vol. 216
PID:
20.500.12556/RUL-138811
UDC:
577.322
ISSN on article:
0141-8130
DOI:
10.1016/j.ijbiomac.2022.06.182
COBISS.SI-ID:
114740483
Publication date in RUL:
19.08.2022
Views:
491
Downloads:
124
Metadata:
Cite this work
Plain text
BibTeX
EndNote XML
EndNote/Refer
RIS
ABNT
ACM Ref
AMA
APA
Chicago 17th Author-Date
Harvard
IEEE
ISO 690
MLA
Vancouver
:
Copy citation
Share:
Record is a part of a journal
Title:
International journal of biological macromolecules
Shortened title:
Int. j. biol. macromol.
Publisher:
Elsevier
ISSN:
0141-8130
COBISS.SI-ID:
25637888
Licences
License:
CC BY-NC-ND 4.0, Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
Link:
http://creativecommons.org/licenses/by-nc-nd/4.0/
Description:
The most restrictive Creative Commons license. This only allows people to download and share the work for no commercial gain and for no other purposes.
Secondary language
Language:
Slovenian
Keywords:
ß-laktoglobulin
,
fibrilizacijski mehanizem
,
pufer specifični efekt
,
sferoidni oligomeri
Projects
Funder:
NIH - National Institutes of Health
Project number:
RM1GM135136
Funder:
Other - Other funder or multiple funders
Funding programme:
Czech Science Foundation
Project number:
GF20-05789L
Funder:
Other - Other funder or multiple funders
Funding programme:
MEYS CR, Instruct-CZ Centre, CIISB
Project number:
LM201812
Similar documents
Similar works from RUL:
Similar works from other Slovenian collections:
Back