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The influence of glycine on ▫$\beta$▫-lactoglobulin amyloid fibril formation – computer simulation study
ID Jaklin, Matej (Avtor), ID Brudar, Sandi (Avtor), ID Hribar-Lee, Barbara (Avtor)

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Izvleček
Amyloids are protein aggregates involved in various protein condensation diseases. Our study aims to investigate the influence of glycine on the fibrillization mechanism of β-lactoglobulin (BLG), a model protein known to form amyloid fibrils from hydrolysed peptides in low pH aqueous solutions. We conducted atomistic molecular dynamics simulations of aqueous solutions of native and unfolded BLG in glycine buffer at pH 2.0. During the simulations we put our focus on analysing protein-protein/buffer interactions, structural electrostatic potential mapping, and the residence times of glycine and glycinium near specific amino acid residues. Glycinium cations were found to preferentially interact with specific protein residues potentially masking the outer disulfide bonds, affecting thiol deprotonation and influencing disulfide scrambling equilibrium. These interactions can potentially hinder hydrolysis and change the fibrillization pathway. Further investigations, such as constant pH MD simulations, simulations on disulfide bounded oligomers are warranted to validate these findings and deepen our understanding of protein aggregation mechanisms.

Jezik:Angleški jezik
Ključne besede:fibrilization, beta-lactoglobulin, amyloids, MD
Vrsta gradiva:Članek v reviji
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:FKKT - Fakulteta za kemijo in kemijsko tehnologijo
Status publikacije:Objavljeno
Različica publikacije:Recenzirani rokopis
Leto izida:2024
Št. strani:13 str.
Številčenje:Vol. , iss.
PID:20.500.12556/RUL-164940 Povezava se odpre v novem oknu
UDK:577.322:544.77.022.524
ISSN pri članku:0942-9352
DOI:10.1515/zpch-2024-0761 Povezava se odpre v novem oknu
COBISS.SI-ID:214767363 Povezava se odpre v novem oknu
Datum objave v RUL:18.11.2024
Število ogledov:65
Število prenosov:12
Metapodatki:XML DC-XML DC-RDF
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Gradivo je del revije

Naslov:Zeitschrift für physikalische Chemie
Skrajšan naslov:Z. phys. Chem.
Založnik:De Gruyter
ISSN:0942-9352
COBISS.SI-ID:15027205 Povezava se odpre v novem oknu

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:fibrilizacija, beta-laktoglobulin, amiloid, MD

Projekti

Financer:NIH - National Institutes of Health
Številka projekta:RM1GM135136
Naslov:Solvation modeling for next-gen biomolecule simulations

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