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Effect of Charge Regulation and Ion-Dipole Interactions on the Selectivity of Protein-Nanoparticle Binding

Barroso da Silva, Fernando Luis (author)
Boström, Mathias (author)
KTH,Flerskalig materialmodellering
Persson, Clas (author)
KTH,Flerskalig materialmodellering
 (creator_code:org_t)
2014-03-31
2014
English.
In: Langmuir. - : American Chemical Society (ACS). - 0743-7463 .- 1520-5827. ; 30:14, s. 4078-4083
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Keyword

Bovine Beta-Lactoglobulin
Complexation
Salt
Macromolecules
Science

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ref (subject category)
art (subject category)

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