izpis_h1_title_alt

Phase stability of aqueous mixtures of bovine serum albumin with low molecular mass salts in presence of polyethylene glycol
ID Džudžević Čančar, Hurija (Author), ID Belak Vivod, Matic (Author), ID Vlachy, Vojko (Author), ID Lukšič, Miha (Author)

.pdfPDF - Presentation file, Download (505,22 KB)
MD5: CDD9DAF3C6870ED22CA7677CDA05688F
URLURL - Source URL, Visit https://www.sciencedirect.com/science/article/pii/S0167732222000125 This link opens in a new window

Abstract
The stability of bovine serum albumin (BSA) solutions against phase separation caused by cooling the system is studied under the combined influence of added poly(ethylene glycol) (PEG) and alkali halide salts in water as solvent. The phase stability of the system depends on the concentration of the added PEG and its molecular mass, the concentration of the low molecular mass electrolyte and its nature, as also on the pH of the solution. More specifically, the addition of NaCl to the BSA-PEG mixture promotes phase separation at pH = 4.0, where BSA carries the net positive charge in aqueous solution, and it increases the stability of the solution at pH = 4.6, i.e., near the isoionic point of the protein. Moreover, at pH = 4.6, the cloud-point temperature decreases in the order from NaF to NaI and from LiCl to CsCl. The order of the salts at pH = 4.0 is exactly reversed: LiCl and NaF show the weakest effect on the cloud-point temperature and the strongest decrease in stability is caused by RbCl and NaNO$_3$. An attempt is made to correlate these observations with the free energies of hydration of the added salt ions and with the effect of adsorption of salt ions on the protein surface on the protein–protein interactions. Kosmotropic salt ions decrease the phase stability of BSA-PEG-salt solutions at pH < pI, while exactly the opposite is true at pH = pI.

Language:English
Keywords:bovine serum albumin solution, polyethylene glycol, cloud–point temperature, solubility, salt specific effects
Work type:Article
Typology:1.01 - Original Scientific Article
Organization:FKKT - Faculty of Chemistry and Chemical Technology
Publication status:Published
Publication version:Version of Record
Year:2022
Number of pages:8 str.
Numbering:Vol. 349, art. 118477
PID:20.500.12556/RUL-137624 This link opens in a new window
UDC:577.322
ISSN on article:0167-7322
DOI:10.1016/j.molliq.2022.118477 This link opens in a new window
COBISS.SI-ID:93209859 This link opens in a new window
Publication date in RUL:23.06.2022
Views:858
Downloads:138
Metadata:XML DC-XML DC-RDF
:
Copy citation
Share:Bookmark and Share

Record is a part of a journal

Title:Journal of molecular liquids
Shortened title:J. mol. liq.
Publisher:Elsevier
ISSN:0167-7322
COBISS.SI-ID:15382277 This link opens in a new window

Licences

License:CC BY-NC-ND 4.0, Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
Link:http://creativecommons.org/licenses/by-nc-nd/4.0/
Description:The most restrictive Creative Commons license. This only allows people to download and share the work for no commercial gain and for no other purposes.

Secondary language

Language:Slovenian
Keywords:goveji serumski albumin, vodne raztopine, fazna stabilnost, polietilen glikol, topnost

Projects

Funder:ARRS - Slovenian Research Agency
Project number:P1-0201
Name:Fizikalna kemija

Funder:ARRS - Slovenian Research Agency
Project number:J1-1708
Name:Raziskave agregacije proteinov v vodnih raztopinah soli in drugih topnih dodatkov

Funder:ARRS - Slovenian Research Agency
Project number:J1-2471
Name:Kemijska karcinogeneza: mehanistični vpogled

Funder:NIH - National Institutes of Health
Funding programme:RM1
Project number:RM1-GM135136
Name:Solvation modeling for next-gen biomolecule simulations

Similar documents

Similar works from RUL:
Similar works from other Slovenian collections:

Back