Lysozyme thermal stability in the presence of cyclodextrins at different pH values

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F25%3A43932951" target="_blank" >RIV/60461373:22340/25:43932951 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S030146222500081X" target="_blank" >https://www.sciencedirect.com/science/article/pii/S030146222500081X</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bpc.2025.107469" target="_blank" >10.1016/j.bpc.2025.107469</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Lysozyme thermal stability in the presence of cyclodextrins at different pH values

Popis výsledku v původním jazyce

In the present study, the primary action of native cyclodextrins (CDs) on lysozyme protein as binding ligand and secondary as aggregation inhibitor were probed. Thermally induced denaturation using differential scanning calorimetry (DSC) was measured in the presence of native α-, β- and γ-CDs. The denaturation process in CD absence was reversible to 60–80 % at pH≤6 with maximum T&lt;inf&gt;m&lt;/inf&gt; at pH=4. Denaturation in the presence of native α-CD at pH from 2 to 10, at the least stable and partially reversible conditions in presence of β-CD and γ-CDs at single pH 2 only, was measured. The protein thermal stability decreases in the presence of CDs, with the most evident for β-CD, followed by α-CD and almost no effect for γ-CD. The reversibility in the presence of α-CD was similar to that in its absence. The best protection performance against heat-induced denaturation was found at pH 2 for β-CD. The heat capacity data for α-CD at acidic pH were fitted by the protein-ligand binding model in the whole temperature and ligand concentration ranges studied. The decrease in thermal stability for α-CD at all pH, β- and γ-CD at pH 2 were fitted linearly as a function of ligand concentration. The CD-to-lysozyme binding parameters obtained in this work and from the literature for other CDs are briefly discussed using the concept of cyclodextrin cavity size, charge distribution, solvent accessible surface area and amino acid hydrophobicity. © 2025 Elsevier B.V.

Název v anglickém jazyce

Lysozyme thermal stability in the presence of cyclodextrins at different pH values

Popis výsledku anglicky

In the present study, the primary action of native cyclodextrins (CDs) on lysozyme protein as binding ligand and secondary as aggregation inhibitor were probed. Thermally induced denaturation using differential scanning calorimetry (DSC) was measured in the presence of native α-, β- and γ-CDs. The denaturation process in CD absence was reversible to 60–80 % at pH≤6 with maximum T&lt;inf&gt;m&lt;/inf&gt; at pH=4. Denaturation in the presence of native α-CD at pH from 2 to 10, at the least stable and partially reversible conditions in presence of β-CD and γ-CDs at single pH 2 only, was measured. The protein thermal stability decreases in the presence of CDs, with the most evident for β-CD, followed by α-CD and almost no effect for γ-CD. The reversibility in the presence of α-CD was similar to that in its absence. The best protection performance against heat-induced denaturation was found at pH 2 for β-CD. The heat capacity data for α-CD at acidic pH were fitted by the protein-ligand binding model in the whole temperature and ligand concentration ranges studied. The decrease in thermal stability for α-CD at all pH, β- and γ-CD at pH 2 were fitted linearly as a function of ligand concentration. The CD-to-lysozyme binding parameters obtained in this work and from the literature for other CDs are briefly discussed using the concept of cyclodextrin cavity size, charge distribution, solvent accessible surface area and amino acid hydrophobicity. © 2025 Elsevier B.V.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

BIOPHYSICAL CHEMISTRY

ISSN

0301-4622

e-ISSN

1873-4200

Svazek periodika

324

Číslo periodika v rámci svazku

september

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

107469

Kód UT WoS článku

001502511000001

EID výsledku v databázi Scopus

2-s2.0-105006487905