Engineering a well-ordered, functional protein-gold nanoparticle assembly.

Abstract:

:The study of interactions between proteins and nanoparticles is important to advancing applications of nanoparticles in biology, medicine, and materials science. Here, we report the encapsulation of a 5-nm diameter gold nanoparticle (AuNP) by thermophilic ferritin (tF), achieved in nearly quantitative yield under mild conditions that preserved the secondary structure, ferroxidase activity, and thermal stability of the native, 4-helix bundle protein subunits. Chromatography-based assays determined that stable protein assembly around AuNPs occurred on long time scales (~48h) and was reversible. Apparent association constants were determined at 25°C for equilibrated tF-BSPP-capped AuNP samples (KA=(2.1±0.4)×10(78)M(-11)) and compared favorably to salt-assembled tF samples (KA=(2.2±0.5)×10(68)M(-11)) at the same protein concentration (0.3mg/mL). Finally, addition of gold ions and mild reducing agent to the tF-AuNP assembly produced 8-nm diameter AuNPs with surface plasmon resonance band unchanged at 520nm, indicative of templating by the protein shell.

journal_name

J Inorg Biochem

authors

Cheung-Lau JC,Liu D,Pulsipher KW,Liu W,Dmochowski IJ

doi

10.1016/j.jinorgbio.2013.10.003

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

59-68

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(13)00267-5

journal_volume

130

pub_type

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