Biomolecular Complexation on the

J 2022

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

SIMONČIČ, Matjaž, Jozef HRITZ a Miha LUKŠIČ

Základní údaje

Originální název

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

Autoři

SIMONČIČ, Matjaž, Jozef HRITZ (703 Slovensko, garant, domácí) a Miha LUKŠIČ

Vydání

Biomacromolecules, American Chemical Society, 2022, 1525-7797

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 6.200

Kód RIV

RIV/00216224:14740/22:00126924

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1021/acs.biomac.2c00933

UT WoS

000859196000001

Klíčová slova anglicky

SPHERICAL POLYELECTROLYTE BRUSHESBETA-LACTOGLOBULINCAPILLARY-ELECTROPHORESISELECTROSTATIC INTERACTIONPERSISTENCE LENGTHCHARGE-REGULATIONPROTEINBINDINGCOACERVATIONADSORPTION

Štítky

CF BIC, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 15. 10. 2024 15:46, Ing. Marie Švancarová

Anotace

V originále

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 (-SO3-) 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.

Návaznosti

EF18_046/0015974, projekt VaV

Název: Modernizace České infrastruktury pro integrativní strukturní biologii

GF20-05789L, projekt VaV

Název: Charakterizace přirozeně neuspořádaných proteinů

Investor: Grantová agentura ČR, Characterization of intrinsically disordered proteins, Partnerská agentura (Rakousko)

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

SIMONČIČ, Matjaž, Jozef HRITZ a Miha LUKŠIČ. 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. Biomacromolecules. American Chemical Society, 2022, roč. 23, č. 10, s. 4412-4426. ISSN 1525-7797. Dostupné z: https://dx.doi.org/10.1021/acs.biomac.2c00933.

@article{2225441,
   author = {Simončič, Matjaž and Hritz, Jozef and Lukšič, Miha},
   article_number = {10},
   doi = {http://dx.doi.org/10.1021/acs.biomac.2c00933},
   keywords = {SPHERICAL POLYELECTROLYTE BRUSHESBETA-LACTOGLOBULINCAPILLARY-ELECTROPHORESISELECTROSTATIC INTERACTIONPERSISTENCE LENGTHCHARGE-REGULATIONPROTEINBINDINGCOACERVATIONADSORPTION},
   language = {eng},
   issn = {1525-7797},
   journal = {Biomacromolecules},
   title = {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},
   url = {https://pubs.acs.org/doi/10.1021/acs.biomac.2c00933},
   volume = {23},
   year = {2022}
}

TY  - JOUR
ID  - 2225441
AU  - Simončič, Matjaž - Hritz, Jozef - Lukšič, Miha
PY  - 2022
TI  - 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
JF  - Biomacromolecules
VL  - 23
IS  - 10
SP  - 4412-4426
EP  - 4412-4426
PB  - American Chemical Society
SN  - 15257797
KW  - SPHERICAL POLYELECTROLYTE BRUSHESBETA-LACTOGLOBULINCAPILLARY-ELECTROPHORESISELECTROSTATIC INTERACTIONPERSISTENCE LENGTHCHARGE-REGULATIONPROTEINBINDINGCOACERVATIONADSORPTION
UR  - https://pubs.acs.org/doi/10.1021/acs.biomac.2c00933
N2  - 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 (-SO3-) 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.
ER  -

SIMONČIČ, Matjaž, Jozef HRITZ a Miha LUKŠIČ. 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. \textit{Biomacromolecules}. American Chemical Society, 2022, roč.~23, č.~10, s.~4412-4426. ISSN~1525-7797. Dostupné z: https://dx.doi.org/10.1021/acs.biomac.2c00933.

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