Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Evolution of Interactions in the Protein Solution As Induced by Mono and Multivalent Ions
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK). Bhabha Atomic Research Centre, India.
Show others and affiliations
Number of Authors: 72019 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 20, no 5, p. 2123-2134Article in journal (Refereed) Published
Abstract [en]

The evolution of interactions in the bovine serum albumin (BSA) protein solution on addition of mono and multivalent (di, tri and tetra) counterions has been studied using small-angle neutron scattering (SANS), dynamic light scattering (DLS) and zeta-potential measurements. It is found that in the presence of mono and divalent counterions, protein behavior can be well explained by DLVO theory, combining the contributions of screened Coulomb repulsion with the van der Waals attraction. The addition of mono or divalent salts in protein solution reduces the repulsive barrier and hence the overall interaction becomes attractive, but the system remains in one-phase for the entire concentration range of the salts, added in the system. However, contrary to DLVO theory, the protein solution undergoes a reentrant phase transition from one-phase to a two-phase system and then back to the one-phase system in the presence of tri and tetravalent counterions. The results show that tri and tetravalent (unlike mono and divalent) counterions induce short-range attraction between the protein molecules, leading to the transformation from one-phase to two-phase system. The two-phase is characterized by the fractal structure of protein aggregates. The excess condensation of these higher-valent counterions in the double layer around the BSA causes the reversal of charge of the protein molecules resulting into reentrant of the one-phase, at higher salt concentrations. The complete phase behavior with mono and multivalent ions has been explained in terms of the interplay of electrostatic repulsion and ion induced short-range attraction between the protein molecules.

Place, publisher, year, edition, pages
2019. Vol. 20, no 5, p. 2123-2134
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:su:diva-170141DOI: 10.1021/acs.biomac.9b00374ISI: 000468120800030PubMedID: 30908911OAI: oai:DiVA.org:su-170141DiVA, id: diva2:1331287
Available from: 2019-06-26 Created: 2019-06-26 Last updated: 2019-06-26Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Kumar, SugamRay, DebesSaha, Debasish
By organisation
Department of Materials and Environmental Chemistry (MMK)
In the same journal
Biomacromolecules
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf