2007
DOI: 10.1007/s11468-007-9033-z
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Tunable Assembly of Peptide-coated Gold Nanoparticles

Abstract: The interaction between peptides and gold surfaces has increasingly been of interest for bionanotechnology applications. To more fully understand how to control such interactions, we have studied the optical properties of peptide-modified gold nanoparticles as a function of peptide composition, pH of the surrounding medium, and peptide concentration. We show using localized surface plasmon resonance, transmission electron microscopy, and surface-enhanced Raman scattering (SERS) that selected "gold-binding pept… Show more

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Cited by 25 publications
(22 citation statements)
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“…35 The spectra displayed minute amounts of noise at higher wavelengths, which is expected for silica gold nanoshells. 36 Nanoshells demonstrated ideal optical properties for near-infrared (NIR) application, 37,38 though such experiments were not included in the scope of this work.…”
Section: Nanoparticle Characterizationmentioning
confidence: 99%
“…35 The spectra displayed minute amounts of noise at higher wavelengths, which is expected for silica gold nanoshells. 36 Nanoshells demonstrated ideal optical properties for near-infrared (NIR) application, 37,38 though such experiments were not included in the scope of this work.…”
Section: Nanoparticle Characterizationmentioning
confidence: 99%
“…The ones selected via cell surface display include gold (Brown 1997) and zinc oxide (Kjaergaard et al 2000), whereas phage display selected ones are for their affinity towards gallium arsenide (Whaley et al 2000), silica (Naik et al 2002a;Eteshola et al 2005), silver (Naik et al 2002b), zinc sulphide (Lee et al 2002a), calcite (Li et al 2002), cadmium sulphide (Mao et al 2003) and titanium oxide (Sano et al 2005). Some biocombinatorially selected peptides have been used to assemble inorganic particles (Whaley et al 2000;Lee et al 2002a,b;Mao et al 2003;Matthes et al 2008) or to control nucleation of the compounds that they were selected for (Li et al 2002;Naik et al 2002a,b;Tullman et al 2008).…”
Section: Genetic Selection and Directed Evolution Of Solid-binding Pementioning
confidence: 99%
“…[6][7][8] Length and charge of the peptide were considered based on the negatively charged surface of the citrate-capped AuNPs. 7,33 It is well known that conjugating with adequate ligands can improve the stability of AuNPs, and the stabilizing effect can be increased with the increase in length of the peptide. However, longer peptides may be broken easily, causing increased background for detection.…”
Section: Discussionmentioning
confidence: 99%
“…Five negatively charged amino acid molecules, namely aspartic acid (D) molecules, conjugated onto the AuNPs colloid, could increase the stability of the peptide-capped AuNPs and avoid AuNPs aggregation by increasing electrostatic repulsion between the peptides. 13,33 Moreover, negative charge on the spacer peptide could allow a well packed layer of peptides on the AuNP surface to increase enzyme access to the cleavage site.…”
Section: Discussionmentioning
confidence: 99%