Colorimetric Protein Sensing by Controlled Assembly of Gold Nanoparticles Functionalized with Synthetic Receptors

被引:98
作者
Aili, Daniel [1 ]
Selegard, Robert [1 ]
Baltzer, Lars [2 ]
Enander, Karin [1 ]
Liedberg, Bo [1 ]
机构
[1] Linkoping Univ, Dept Phys Chem & Biol IFM, SE-58183 Linkoping, Sweden
[2] Uppsala Univ, Dept Biochem & Organ Chem, BMC, SE-75123 Uppsala, Sweden
基金
瑞典研究理事会;
关键词
bioassays; gold; helical structures; hybrid materials; nanoparticles; CARBONIC-ANHYDRASE-II; SURFACE-PLASMON RESONANCE; OPTICAL-PROPERTIES; IMMUNOASSAY; BINDING; RECOGNITION; KINETICS; DESIGN; ASSAY;
D O I
10.1002/smll.200900530
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A novel strategy is described for the colorimetric sensing of proteins, based on polypeptide-functionalized gold nanoparticles. Recognition is accomplished using a polypeptide sensor scaffold designed to specifically bind to the model analyte, human carbonic anhydrase II (HCAII). The extent of particle aggregation, induced by the Zn2+-triggered dimerization and folding of a second polypeptide also present on the surface of the gold nanoparticle, gives a readily detectable colorimetric shift that is dependent on the concentration of the target protein. In the absence of HCAII, particle aggregation results in a major redshift of the plasmon peak, whereas analyte binding prevented the formation of dense aggregates, significantly reducing the magnitude of the redshift. The versatility of the technique is demonstrated using a second model system based on the recognition of a peptide sequence from the tobacco mosaic virus coat protein (TMVP) by a recombinant antibody fragment (Fab57P). Concentrations down to approximate to 10 nM and approximate to 25 nM are detected for HCAII and Fab57P, respectively. This strategy is proposed as a generic platform for robust and specific protein analysis that can be further developed to monitor a wide range of target proteins.
引用
收藏
页码:2445 / 2452
页数:8
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