Influence of Nanoparticle Size on the PH-dependent Structure of Adsorbed Proteins Studied with Quantitative Localized Surface Plasmon Spectroscopy

Overview

Journal Eur Phys J E Soft Matter

Publisher EDP Sciences

Specialty Biophysics

Date 2009 Mar 10

PMID 19267244

Authors

J H Teichroeb

P Z McVeigh

J A Forrest

Affiliations

Soon will be listed here.

Abstract

We have studied pH-dependent conformational transitions of Bovine Serum Albumin adsorbed onto different sizes of gold nanospheres. For larger spheres (D > 10 nm) there is evidence for a path-dependent extended state near pH 4, over a very small pH range. For smaller nanospheres (5 nm and 10 nm) the evidence for such a transition is either much weaker or completely suppressed. We suggest that the absence of the transition on small spheres is due to the fact that the protein adsorbed on such small spheres has already lost at least some of its tertiary structure. The results have important implications for the functionality of proteins adsorbed onto nanospheres or surfaces with nm scale roughness.

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