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Biomolecular complexation on the “wrong side” : a case study of the influence of salts and sugars on the interactions between bovine serum albumin and sodium polystyrene sulfonate
ID
Simončič, Matjaž
(
Author
),
ID
Hritz, Jozef
(
Author
),
ID
Lukšič, Miha
(
Author
)
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MD5: 102BF10C334F8E0CEDB2FB6B68FFD778
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https://pubs.acs.org/doi/10.1021/acs.biomac.2c00933
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Abstract
In the protein purification, drug delivery, food industry, and biotechnological applications involving protein−polyelectrolyte complexation, proper selection of co-solutes and solution conditions plays a crucial role. The onset of (bio)macromolecular complexation occurs even on the so-called “wrong side” of the protein isoionic point where both the protein and the polyelectrolyte are net like-charged. To gain mechanistic insights into the modulatory role of salts (NaCl, NaBr, and NaI) and sugars (sucrose and sucralose) in protein−polyelectrolyte complexation under such conditions, interaction between bovine serum albumin (BSA) and sodium polystyrene sulfonate (NaPSS) at pH = 8.0 was studied by a combination of isothermal titration calorimetry, fluorescence spectroscopy, circular dichroism, and thermodynamic modeling. The BSA−NaPSS complexation proceeds by two binding processes (first, formation of intrapolymer complexes and then formation of interpolymer complexes), both driven by favorable electrostatic interactions between the negatively charged sulfonic groups (−SO$_3^−$) of NaPSS and positively charged patches on the BSA surface. Two such positive patches were identified, each responsible for one of the two binding processes. The presence of salts screened both short-range attractive and long-range repulsive electrostatic interactions between both macromolecules, resulting in a nonmonotonic dependence of the binding affinity on the total ionic strength for both binding processes. In addition, distinct anion-specific effects were observed (NaCl < NaBr < NaI). The effect of sugars was less pronounced: sucrose had no effect on the complexation, but its chlorinated analogue, sucralose, promoted it slightly due to the screening of long-range repulsive electrostatic interactions between BSA and NaPSS. Although short-range non-electrostatic interactions are frequently mentioned in the literature in relation to BSA or NaPSS, we found that the main driving force of complexation on the “wrong side” are electrostatic interactions.
Language:
English
Keywords:
protein-polyelectrolyte complexation
,
sucrose
,
sucralose
,
electrostatic interactions
,
salt-specific effects
,
carbohydrates
,
complexation
,
ionic strength
,
salts
,
titration
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:
Str. 4412–4426
Numbering:
Vol. 23, iss. 10
PID:
20.500.12556/RUL-141995
UDC:
577.322
ISSN on article:
1525-7797
DOI:
10.1021/acs.biomac.2c00933
COBISS.SI-ID:
122596099
Publication date in RUL:
14.10.2022
Views:
578
Downloads:
145
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Record is a part of a journal
Title:
Biomacromolecules
Publisher:
American Chemical Society
ISSN:
1525-7797
COBISS.SI-ID:
22445317
Licences
License:
CC BY 4.0, Creative Commons Attribution 4.0 International
Link:
http://creativecommons.org/licenses/by/4.0/
Description:
This is the standard Creative Commons license that gives others maximum freedom to do what they want with the work as long as they credit the author.
Secondary language
Language:
Slovenian
Keywords:
kompleksacija protein-polielektrolit
,
saharoza
,
sukraloza
,
elektrostatske interakcije
,
ionospecifični efekti
Projects
Funder:
Other - Other funder or multiple funders
Funding programme:
MEYS CR
Project number:
LM2018127
Funder:
EC - European Commission
Funding programme:
European Regional Development Fund
Project number:
CZ.02.1.01/0.0/0.0/18_046/0015974
Acronym:
UP CIISB
Funder:
ARRS - Slovenian Research Agency
Project number:
P1-0201
Name:
Fizikalna kemija
Funder:
ARRS - Slovenian Research Agency
Funding programme:
Young researchers
Funder:
NIH - National Institutes of Health
Funding programme:
RM1
Project number:
RM1GM135136
Name:
Solvation modeling for next-gen biomolecule simulations
Funder:
Other - Other funder or multiple funders
Funding programme:
Czech Science Foundation
Project number:
GF20-05789L
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