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Influence of low molecular weight salts on the viscosity of aqueous-buffer bovine serum albumin solutions
ID
Zdovc, Blaž
(
Avtor
),
ID
Jaklin, Matej
(
Avtor
),
ID
Hribar-Lee, Barbara
(
Avtor
),
ID
Lukšič, Miha
(
Avtor
)
PDF - Predstavitvena datoteka,
prenos
(593,99 KB)
MD5: CFC7AEE2D61CDEB1088E2ED7C7F502D1
URL - Izvorni URL, za dostop obiščite
https://www.mdpi.com/1420-3049/27/3/999
Galerija slik
Izvleček
Pharmaceutical design of protein formulations aims at maximum efficiency (protein concentration) and minimum viscosity. Therefore, it is important to know the nature of protein-protein interactions and their influence on viscosity. In this work, we investigated the dependence of the viscosity of BSA in an aqueous 20 mM acetate buffer at pH = 4.3 on protein concentration and on temperature (5–45 °C). The viscosity of the solution increased with protein concentration and was 230% higher than the viscosity of the protein-free formulation at 160 mg/mL. The viscosity decreased by almost 60% in the temperature range from 5 to 45 °C. The agreement of the modified Arrhenius theory with experiment was quantitative, whereas a hard-sphere model provided only a qualitative description of the experimental results. We also investigated the viscosity of a 100 mg/mL BSA solution as a function of the concentration of added low molecular weight salts (LiCl, NaCl, KCl, RbCl, CsCl, NaBr, NaI) in the range of salt concentrations up to 1.75 mol/L. In addition, the particle size and zeta potential of BSA-salt mixtures were determined for solutions containing 0.5 mol/L salt. The trends with respect to the different anions followed a direct Hofmeister series (Cl$^–$ > Br$^–$ > I$^–$), whereas for cations in the case of viscosity the indirect Hofmeister series was observed (Li$^+$ > Na$^+$ > K$^+$ > Rb$^+$ > Cs$^+$), but the values of particle sizes and zeta potential did not show cation-specific effects. Since the protein is positively charged at pH = 4.3, anions are more attracted to the protein surface and shield its charge, while the interaction with cations is less pronounced. We hypothesize that salt surface charge shielding reduces protein colloidal stability and promotes protein aggregate formation.
Jezik:
Angleški jezik
Ključne besede:
bovine serum albumin
,
viscosity
,
zeta-potential
,
ion-specific effects
,
protein aggregation
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:
2022
Št. strani:
16 str.
Številčenje:
Vol. 27, iss. 3, art. 999
PID:
20.500.12556/RUL-136984
UDK:
577.322
ISSN pri članku:
1420-3049
DOI:
10.3390/molecules27030999
COBISS.SI-ID:
96153859
Datum objave v RUL:
27.05.2022
Število ogledov:
887
Število prenosov:
138
Metapodatki:
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Objavi na:
Gradivo je del revije
Naslov:
Molecules
Skrajšan naslov:
Molecules
Založnik:
MDPI
ISSN:
1420-3049
COBISS.SI-ID:
18462981
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:
01.02.2022
Sekundarni jezik
Jezik:
Slovenski jezik
Ključne besede:
proteini
,
goveji serumski albumin
,
soli
,
viskoznost
,
zeta potencial
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:
J1-1708
Naslov:
Raziskave agregacije proteinov v vodnih raztopinah soli in drugih topnih dodatkov
Financer:
ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:
J1-2471
Naslov:
Kemijska karcinogeneza: mehanistični vpogled
Financer:
NIH - National Institutes of Health
Številka projekta:
RM1-GM135136
Naslov:
Solvation modeling for next-gen biomolecule simulations
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