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Effect of Charge Regulation and Ion-Dipole Interactions on the Selectivity of Protein-Nanoparticle Binding
KTH, Skolan för industriell teknik och management (ITM), Materialvetenskap, Flerskalig materialmodellering.
KTH, Skolan för industriell teknik och management (ITM), Materialvetenskap, Flerskalig materialmodellering.ORCID-id: 0000-0002-9050-5445
2014 (engelsk)Inngår i: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 30, nr 14, s. 4078-4083Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
American Chemical Society (ACS), 2014. Vol. 30, nr 14, s. 4078-4083
Emneord [en]
Bovine Beta-Lactoglobulin, Complexation, Salt, Macromolecules, Science
HSV kategori
Identifikatorer
URN: urn:nbn:se:kth:diva-145584DOI: 10.1021/la500027fISI: 000334657800020Scopus ID: 2-s2.0-84898888317OAI: oai:DiVA.org:kth-145584DiVA, id: diva2:719332
Forskningsfinansiär
Swedish Research Council, C0485101Swedish Energy Agency, 34138-1
Merknad

QC 20140523

Tilgjengelig fra: 2014-05-23 Laget: 2014-05-23 Sist oppdatert: 2017-12-05bibliografisk kontrollert

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