The role of buffers in wild-type HEWL amyloid fibril formation mechanism

Brudar, Sandi (avtor), Hribar-Lee, Barbara (avtor)

Amyloid fibrils, highly ordered protein aggregates, play an important role in the onset of several neurological disorders. Many studies have assessed amyloid fibril formation under specific solution conditions, but they all lack an important phenomena in biological solutions—buffer specific effects. We have focused on the formation of hen egg-white lysozyme (HEWL) fibrils in aqueous solutions of different buffers in both acidic and basic pH range. By means of UV-Vis spectroscopy, fluorescence measurements and CD spectroscopy, we have managed to show that fibrillization of HEWL is affected by buffer identity (glycine, TRIS, phosphate, KCl-HCl, cacodylate, HEPES, acetate), solution pH, sample incubation (agitated vs. static) and added excipients (NaCl and PEG). HEWL only forms amyloid fibrils at pH = 2.0 under agitated conditions in glycine and KCl-HCl buffers of high enough ionic strength. Phosphate buffer on the other hand stabilizes the HEWL molecules. Similar stabilization effect was achieved by addition of PEG12000 molecules to the solution.

• Jezik: Angleški jezik
• Ključne besede: lysozyme, amyloid fibrils, buffer-specific effects
• 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: 2019
• Št. strani: 18 str.
• Številčenje: Vol. 9, iss. 2, art. 65
• PID: 20.500.12556/RUL-125374
• UDK: 577.322
• ISSN pri članku: 2218-273X
• DOI: 10.3390/biom9020065
• COBISS.SI-ID: 1538128835
• Datum objave v RUL: 12.03.2021

BRUDAR, Sandi in HRIBAR-LEE, Barbara, 2019, The role of buffers in wild-type HEWL amyloid fibril formation mechanism. Biomolecules [na spletu]. 2019. Vol. 9, no. 2,  65. [Dostopano 3 maj 2025]. DOI 10.3390/biom9020065. Pridobljeno s: https://repozitorij.uni-lj.si/IzpisGradiva.php?lang=slv&id=125374

Gradivo je del revije

• Naslov: Biomolecules
• Skrajšan naslov: Biomolecules
• Založnik: MDPI AG
• ISSN: 2218-273X
• COBISS.SI-ID: 519952921

Licence

• Licenca: CC BY 4.0, Creative Commons Priznanje avtorstva 4.0 Mednarodna
• Povezava: http://creativecommons.org/licenses/by/4.0/deed.sl
• Opis: To je standardna licenca Creative Commons, ki daje uporabnikom največ možnosti za nadaljnjo uporabo dela, pri čemer morajo navesti avtorja.
• Začetek licenciranja: 12.03.2021

Sekundarni jezik

• Jezik: Slovenski jezik
• Ključne besede: lizocim, amiloidne fibrile, pufer-specifični efekti

Projekti

• Financer: ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
• Številka projekta: P1-0201
• Naslov: Fizikalna kemija

• Financer: ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
• Številka projekta: BI-US/18-19-061