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Effect of Charge Regulation and Ion-Dipole Interactions on the Selectivity of Protein-Nanoparticle Binding
KTH, School of Industrial Engineering and Management (ITM), Materials Science and Engineering, Multiscale Materials Modelling.
KTH, School of Industrial Engineering and Management (ITM), Materials Science and Engineering, Multiscale Materials Modelling.ORCID iD: 0000-0002-9050-5445
2014 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 30, no 14, 4078-4083 p.Article in journal (Refereed) Published
Abstract [en]

We investigate the role of different mesoscopic interactions (Coulomb, charge regulation, and ion-dipole "surface patch" effects) on the binding of bovine serum albumin (BSA) and beta-lactoglobulin (BLG) to a cationic gold nanoparticle (TTMA+). The results demonstrate that the charge-regulation mechanism plays a vital role for selectivity of protein-nanoparticle complexation at low salt concentration. At slightly higher ionic strengths, charge-dipole effects are the dominating driving force. Thus, very small variations in salt concentration strongly influence the origin of complexation.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2014. Vol. 30, no 14, 4078-4083 p.
Keyword [en]
Bovine Beta-Lactoglobulin, Complexation, Salt, Macromolecules, Science
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:kth:diva-145584DOI: 10.1021/la500027fISI: 000334657800020Scopus ID: 2-s2.0-84898888317OAI: oai:DiVA.org:kth-145584DiVA: diva2:719332
Funder
Swedish Research Council, C0485101Swedish Energy Agency, 34138-1
Note

QC 20140523

Available from: 2014-05-23 Created: 2014-05-23 Last updated: 2017-12-05Bibliographically approved

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Persson, Clas

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