Effect of Charge Regulation and Ion-Dipole Interactions on the Selectivity of Protein-Nanoparticle Binding
2014 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 30, no 14, 4078-4083 p.Article in journal (Refereed) Published
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.
Bovine Beta-Lactoglobulin, Complexation, Salt, Macromolecules, Science
Engineering and Technology
IdentifiersURN: urn:nbn:se:kth:diva-145584DOI: 10.1021/la500027fISI: 000334657800020ScopusID: 2-s2.0-84898888317OAI: oai:DiVA.org:kth-145584DiVA: diva2:719332
FunderSwedish Research Council, C0485101Swedish Energy Agency, 34138-1
QC 201405232014-05-232014-05-232014-05-23Bibliographically approved