A new fibrillization mechanism of β-lactoglobulin in glycine
solutions

J 2022

A new fibrillization mechanism of β-lactoglobulin in glycine solutions

JAKLIN, M., Jozef HRITZ a B. HRIBAR-LEE

Základní údaje

Originální název

A new fibrillization mechanism of β-lactoglobulin in glycine solutions

Autoři

JAKLIN, M., Jozef HRITZ (703 Slovensko, garant, domácí) a B. HRIBAR-LEE

Vydání

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, NETHERLANDS, ELSEVIER, 2022, 0141-8130

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 8.200

Kód RIV

RIV/00216224:14740/22:00126925

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.ijbiomac.2022.06.182

UT WoS

000863069300002

Klíčová slova anglicky

beta-lactoglobulinfl-lactoglobulin; FibrillizationBuffer; specific effects;Spheroid oligomers

Štítky

CF BIC, CF NANO, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 15. 10. 2024 11:07, Ing. Monika Szurmanová, Ph.D.

Anotace

V originále

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 beta-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.

Návaznosti

GF20-05789L, projekt VaV

Název: Charakterizace přirozeně neuspořádaných proteinů

Investor: Grantová agentura ČR, Characterization of intrinsically disordered proteins, Partnerská agentura (Rakousko)

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

JAKLIN, M., Jozef HRITZ a B. HRIBAR-LEE. A new fibrillization mechanism of β-lactoglobulin in glycine solutions. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES. NETHERLANDS: ELSEVIER, 2022, roč. 216, SEP, s. 414-425. ISSN 0141-8130. Dostupné z: https://dx.doi.org/10.1016/j.ijbiomac.2022.06.182.

@article{2225442,
   author = {Jaklin, M. and Hritz, Jozef and HribarandLee, B.},
   article_location = {NETHERLANDS},
   article_number = {SEP},
   doi = {http://dx.doi.org/10.1016/j.ijbiomac.2022.06.182},
   keywords = {beta-lactoglobulinfl-lactoglobulin; FibrillizationBuffer; specific effects;Spheroid oligomers},
   language = {eng},
   issn = {0141-8130},
   journal = {INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES},
   title = {A new fibrillization mechanism of β-lactoglobulin in glycine solutions},
   url = {https://www.sciencedirect.com/science/article/pii/S0141813022013952?via%3Dihub},
   volume = {216},
   year = {2022}
}

TY  - JOUR
ID  - 2225442
AU  - Jaklin, M. - Hritz, Jozef - Hribar-Lee, B.
PY  - 2022
TI  - A new fibrillization mechanism of β-lactoglobulin in glycine solutions
JF  - INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
VL  - 216
IS  - SEP
SP  - 414-425
EP  - 414-425
PB  - ELSEVIER
SN  - 01418130
KW  - beta-lactoglobulinfl-lactoglobulin
KW  - FibrillizationBuffer
KW  - specific effects;Spheroid oligomers
UR  - https://www.sciencedirect.com/science/article/pii/S0141813022013952?via%3Dihub
N2  - 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 beta-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.
ER  -

JAKLIN, M., Jozef HRITZ a B. HRIBAR-LEE. A new fibrillization mechanism of β-lactoglobulin in glycine solutions. \textit{INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES}. NETHERLANDS: ELSEVIER, 2022, roč.~216, SEP, s.~414-425. ISSN~0141-8130. Dostupné z: https://dx.doi.org/10.1016/j.ijbiomac.2022.06.182.

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