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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
(
Avtor
),
ID
Hritz, Jozef
(
Avtor
),
ID
Lukšič, Miha
(
Avtor
)
PDF - Predstavitvena datoteka,
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(2,63 MB)
MD5: 102BF10C334F8E0CEDB2FB6B68FFD778
URL - Izvorni URL, za dostop obiščite
https://pubs.acs.org/doi/10.1021/acs.biomac.2c00933
Galerija slik
Izvleček
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.
Jezik:
Angleški jezik
Ključne besede:
protein-polyelectrolyte complexation
,
sucrose
,
sucralose
,
electrostatic interactions
,
salt-specific effects
,
carbohydrates
,
complexation
,
ionic strength
,
salts
,
titration
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:
Str. 4412–4426
Številčenje:
Vol. 23, iss. 10
PID:
20.500.12556/RUL-141995
UDK:
577.322
ISSN pri članku:
1525-7797
DOI:
10.1021/acs.biomac.2c00933
COBISS.SI-ID:
122596099
Datum objave v RUL:
14.10.2022
Število ogledov:
584
Število prenosov:
146
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Objavi na:
Gradivo je del revije
Naslov:
Biomacromolecules
Založnik:
American Chemical Society
ISSN:
1525-7797
COBISS.SI-ID:
22445317
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.
Sekundarni jezik
Jezik:
Slovenski jezik
Ključne besede:
kompleksacija protein-polielektrolit
,
saharoza
,
sukraloza
,
elektrostatske interakcije
,
ionospecifični efekti
Projekti
Financer:
Drugi - Drug financer ali več financerjev
Program financ.:
MEYS CR
Številka projekta:
LM2018127
Financer:
EC - European Commission
Program financ.:
European Regional Development Fund
Številka projekta:
CZ.02.1.01/0.0/0.0/18_046/0015974
Akronim:
UP CIISB
Financer:
ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:
P1-0201
Naslov:
Fizikalna kemija
Financer:
ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Program financ.:
Young researchers
Financer:
NIH - National Institutes of Health
Program financ.:
RM1
Številka projekta:
RM1GM135136
Naslov:
Solvation modeling for next-gen biomolecule simulations
Financer:
Drugi - Drug financer ali več financerjev
Program financ.:
Czech Science Foundation
Številka projekta:
GF20-05789L
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