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 and Miha LUKŠIČ

Basic information

Original name

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

Authors

SIMONČIČ, Matjaž, Jozef HRITZ (703 Slovakia, guarantor, belonging to the institution) and Miha LUKŠIČ

Edition

Biomacromolecules, American Chemical Society, 2022, 1525-7797

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 6.200

RIV identification code

RIV/00216224:14740/22:00126924

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000859196000001

Keywords in English

SPHERICAL POLYELECTROLYTE BRUSHESBETA-LACTOGLOBULINCAPILLARY-ELECTROPHORESISELECTROSTATIC INTERACTIONPERSISTENCE LENGTHCHARGE-REGULATIONPROTEINBINDINGCOACERVATIONADSORPTION

Abstract

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.

Links

EF18_046/0015974, research and development project

Name: Modernizace České infrastruktury pro integrativní strukturní biologii

GF20-05789L, research and development project

Name: Charakterizace přirozeně neuspořádaných proteinů

Investor: Czech Science Foundation, Partner Agency (Austria)

90127, large research infrastructures

Name: CIISB II

Citovat

SIMONČIČ, Matjaž, Jozef HRITZ and 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, vol. 23, No 10, p. 4412-4426. ISSN 1525-7797. Available from: 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 and 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, vol.~23, No~10, p.~4412-4426. ISSN~1525-7797. Available from: https://dx.doi.org/10.1021/acs.biomac.2c00933.

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