Ethylene Glycol‐Protected Magnetic Nanoparticles for a Multiplexed Immunoassay in Human Plasma

Lin, Po‐Chiao; Chou, Po-Hung; Chen, Shuhua; Liao, Hsin-Kai; Wang, Kaiyi; Chen, Yu‐Ju; Lin, Chun‐Cheng

doi:10.1002/smll.200500387

Cited by 144 publications

(117 citation statements)

References 27 publications

Supporting

Mentioning

114

Contrasting

Order By: Relevance

“…However, a recent report showed that the use of a short-chain methyl ethylene glycol on the AuNP surface prevented AuNP aggregation [47] and suppressed nonspecific interactions. [48] Thus, 3-[2-(2-methoxy-ethoxy)ethoxy]propane-1-thiol (MEG) [48] was used as the matrix on the chip to prevent the nonspecific interaction with P k -AuNP. We found that a reliable chip for the competition binding assay could be generated by forming a self-assembled monolayer by using a mixture that contained 40 % thiolated P k ligand and 60 % of MEG as a matrix on a J1 biosensor chip.…”

Section: Multivalent Interactions Of P K -Aunps With B-sltmentioning

confidence: 99%

Globotriose‐Functionalized Gold Nanoparticles as Multivalent Probes for Shiga‐like Toxin

et al. 2008

Self Cite

View full text Add to dashboard Cite

Compared to monovalent carbohydrates, multivalent carbohydrate ligands exhibit significantly enhanced binding affinities to their interacting proteins. Here, we report globotriose (P(k) ligand)-functionalized gold nanoparticle (AuNP) probes for the investigation of multivalent interactions with the B(5) subunit of Shiga-like toxin I (B-Slt). Six P(k)-ligand-encapsulated AuNPs (P(k)-AuNPs) of varying particle size and linker length were synthesized and evaluated for their potential as multivalent affinity probes by using a surface plasmon resonance competition assay. The affinity of these probes for the interacting proteins was greatly affected by nanoparticle size, linker length, and ligand density on nanoparticle surface. For example, the 20-nm 20-P(k)-l-AuNP, which had a relatively long linker showed a >10(8)-fold increase in affinity compared with the mono P(k) ligand. This intrinsic high-affinity AuNP probe specifically captured the recombinant B-Slt from Escherichia coli lysate, and the resulting purity of the B-Slt was >95 %. We also developed a robust P(k)-AuNP-based detection method for Slt-I by combining the technique with silver enhancement.

show abstract

Section: Multivalent Interactions Of P K -Aunps With B-sltmentioning

confidence: 99%

Globotriose‐Functionalized Gold Nanoparticles as Multivalent Probes for Shiga‐like Toxin

et al. 2008

Self Cite

View full text Add to dashboard Cite

show abstract

“…This method allows the MALDI MS detection of low concentration of proteins in complex matrix solution. Other types of nanoparticles have also been used to capture the analytes of interest, such as phosphopeptides [30,31], antigen [32][33][34], oligonucleotides [35,36], aminothiol [37], protein [38,39], and bacteria [40,41]. Among the nanoparticles used, carbon nanotube [38], Nile red-adsorbed gold [37], and TiO 2 -coated magnetic nanoparticles [30] were not only employed as affinity probes but also as matrices.…”

mentioning

confidence: 99%

Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS

Chang

Zheng

Chen

et al. 2007

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

Iron oxide nanoparticles modified with oleate have been employed for the extraction of peptides and proteins from aqueous solution before matrix-assisted laser desorption/ionization (MALDI) mass spectrometric (MS) analysis. Adsorption of peptides and proteins onto the nanoparticles were mainly through electrostatic attraction and hydrophobic interaction. The analyte-adsorbed iron oxide nanoparticles could be efficiently collected from solution using a magnet. No elution step was needed. With this preconcentration strategy, the lowest detectable concentration of angiotensin I, insulin, and myoglobin in 500 L of aqueous solution were 0.1 nM, 0.1 nM, and 10.0 nM, respectively. In addition, the nanoparticles could extract the analytes from solution with a high content of salt and surfactant, thus eliminating suppression effect during MALDI MS analysis. This method was successfully applied to concentrate the tryptic digest products of cytochrome c. In addition, the tryptic digestion of cytochrome c can be directly conducted on the iron oxide nanoparticles. atrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) has become a routine analytical tool to determine the molecular mass of biomolecules [1][2][3]. However, samples containing excessive amounts of salts, surfactants, or other contaminations suffer from ionization suppression and adduct formation [4,5]. This limits the application of MALDI technique. Therefore, a simple and selective procedure for extraction and concentration of analyte from complex samples before MALDI MS is required.Various methods have been developed to isolate the analyte from complex sample matrix. In surface-enhanced laser desorption/ionization (SELDI), the sample target played an active role in the extraction, purification, or concentration of the analyte of interest [6 -9]. The target surface was derivatized for the selective retention of analyte while removing interferences through on-target washing. Several surface derivatizations have been designed to extract and concentrate the analyte through hydrophobic interaction [10,11], ionic interaction [12,13], or immunoaffinity [14,15]. However, the sensitivity improvement was limited by the number of binding sites on the target. In another approach, the so-called surface-enhanced affinity capture (SEAC), micrometer-sized beads made for chromatography column were used to capture peptides and proteins from sample solution [16]. Various types of beads have been used, which include reverse-phase chromatographic beads [17,18] and immobilized metal ion beads [19 -21]. To speed up the collection of analyteadsorbed beads from sample solution, magnetic particles, which can be simply collected using a magnet, were developed [22][23][24]. After collection, the microbeads were washed and placed on sample target, followed by analyzing with MALDI MS. Unfortunately, the presence of those particles on the sample target was reported to cause decrease in mass accuracy and resolution [25,26].Recently, nanoparticles have become interesting p...

show abstract

“…For example, magnetic NPs conjugated with antibodies have been used as affinity probes with mass spectrometric analysis to profile biomarker proteins in human plasma. 38 A multiplexed immunoassay was constructed using various antibody-conjugated NPs. Serum amyloid P (SAP), C-reactive protein (CRP) and serum amyloid A (SAA) in 1 mL of human plasma were selectively and simultaneously captured, separated and analyzed by MALDI-MS. Methoxyethyl-terminated ethylene glycol (MEG) ligands grafted on the NP surfaces together with the antibodies significantly suppressed non-specific binding during the separation of the protein biomarkers.…”

Section: Functionalized Nps For Selective Extraction and Concentrationmentioning

confidence: 99%

Engineered nanoparticle surfaces for improved mass spectrometric analyses

Zhu

Rotello

Vachet

2009

Analyst

View full text Add to dashboard Cite

Ethylene Glycol‐Protected Magnetic Nanoparticles for a Multiplexed Immunoassay in Human Plasma

Cited by 144 publications

References 27 publications

Globotriose‐Functionalized Gold Nanoparticles as Multivalent Probes for Shiga‐like Toxin

Globotriose‐Functionalized Gold Nanoparticles as Multivalent Probes for Shiga‐like Toxin

Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS

Engineered nanoparticle surfaces for improved mass spectrometric analyses

Contact Info

Product

Resources

About