Use of Multiple Peptide-Based SERS Probes Binding to Different Epitopes on a Protein Biomarker To Improve Detection Sensitivity

Shin, Kayeong; Cho, Jun‐Haeng; Yoon, Mi Young; Chung, Hoeil

doi:10.1021/acs.analchem.5b04873

Cited by 13 publications

(8 citation statements)

References 33 publications

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“…For example, compared with naked Au nanoparticles, enzyme-induced silver deposition could enhance the SERS signal four times [16]. Multiple SERS tags, attaching intrinsically strong Raman scattering molecules (called Raman reporters) to the surface of plasmon-resonant nanoparticles, binding to different epitopes on a protein biomarker was also reported to improve the detection sensitivity [17]. It is clear that the efficiency of detection was affected by the preparation steps.…”

Section: Introductionmentioning

confidence: 99%

Ag@Au Core–Shell Porous Nanocages with Outstanding SERS Activity for Highly Sensitive SERS Immunoassay

Huang

Lin

et al. 2019

Sensors

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A highly sensitive immunoassay of biomarkers has been achieved using 4-mercaptobenzoic acid-labeled Ag@Au core–shell porous nanocage tags and α-fetoprotein immuno-sensing chips. The Ag@Au porous nanocages were uniquely synthesized by using an Ag core as a self-sacrificial template and reducing agent, where the slow reaction process led to the formation of a porous Au layer. The size of the remaining Ag core and surface roughness of the Au shell were controlled by adjusting the chloroauric acid concentration. The porous cage exhibited excellent surface-enhanced Raman spectroscopy (SERS) activity, presumably due to a synergetic interaction between newly generated hot spots in the rough Au shell and the retained SERS activity of the Ag core. Using α-fetoprotein as a model analyte for immunoassay, the SERS signal had a wide linear range of 0.20 ng mL−1 to 500.0 ng mL−1 with a detection limit of 0.12 ng mL−1. Without the need of further signal amplification, the as-prepared Ag@Au bimetallic nanocages can be directly used for highly sensitive SERS assays of other biomarkers in biomedical research, diagnostics, etc.

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Section: Introductionmentioning

confidence: 99%

Ag@Au Core–Shell Porous Nanocages with Outstanding SERS Activity for Highly Sensitive SERS Immunoassay

Huang

Lin

et al. 2019

Sensors

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“…Therefore, it is very urgent to improve the detection sensitivity against specific low-abundant protein biomarkers. Enormous progress has been made in the development of analytical technologies for sensitive protein detection, such as the microfluidics, electrochemiluminescent assay, and surface enhanced Raman scattering …”

mentioning

confidence: 99%

“…Enormous progress has been made in the development of analytical technologies for sensitive protein detection, such as the microfluidics, 7 electrochemiluminescent assay, 8 and surface enhanced Raman scattering. 9 Mass spectrometry (MS) is becoming one of the most widely used methods for biomolecule detection, due to the fact that it provides several advantages over other analytical methods, such as high sensitivity and throughput. MS coupled with soft ionization methods possess a unique property of providing the intact molecular weight of analytes, which enables identifications of biological molecules.…”

mentioning

confidence: 99%

Ultrasensitive Detection of Low-Abundance Protein Biomarkers by Mass Spectrometry Signal Amplification Assay

Zhu

Gan

et al. 2016

Anal. Chem.

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A mass spectrometry signal amplification method is developed for the ultrasensitive and selective detection of low-abundance protein biomarkers by utilizing tag molecules on gold nanoparticles (AuNPs). EpCAM and thrombin as model targets are captured by specific aptamers immobilized on the AuNPs. With laser desorption/ionization time-of-flight mass spectrometry (LDI-TOF MS), the mass tag molecules are detected to represent the protein biomarkers. Benefiting from the MS signal amplification, the assay can achieve a limit of detection of 100 aM. The method is further applied to detect thrombin in fetal bovine serum and EpCAM in cell lysates to demonstrate its selectivity and feasibility in complex biological samples. With the high sensitivity and specificity, the protocol shows great promise for providing a new route to single-cell analysis and early disease diagnosis.

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“…The molecular packing on the surface was particularly significant when the OVA coating concentration was high, and there were many antibodies on the ELISA plate surface. 45 The BAP-Loop-Y/pG 2 pA-Y copolymer showed remarkably higher absorbance than the BAP-Y/pG 2 pA-Y copolymers when there was a high OVA coating concentration.…”

Section: ■ Results and Discussionmentioning

confidence: 89%

“…Also, the linear structures of BAP-Loop-Y/pG 2 pA-Y copolymers provide better molecular packing on the surface of the ELISA plate than the 3-dimensional highly branched BAP-Y/pG 2 pA-Y copolymer, resulting in a higher signal in the ELISA. The molecular packing on the surface was particularly significant when the OVA coating concentration was high, and there were many antibodies on the ELISA plate surface . The BAP-Loop-Y/pG 2 pA-Y copolymer showed remarkably higher absorbance than the BAP-Y/pG 2 pA-Y copolymers when there was a high OVA coating concentration.…”

Section: Results and Discussionmentioning

confidence: 98%

Linear Polymerization of Protein by Sterically Controlled Enzymatic Cross-Linking with a Tyrosine-Containing Peptide Loop

et al. 2020

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The structure of a protein complex needs to be controlled appropriately to maximize its functions. Herein, we report the linear polymerization of bacterial alkaline phosphatase (BAP) through the site-specific cross-linking reaction catalyzed by Trametes sp. laccase (TL). We introduced a peptide loop containing a tyrosine (Y-Loop) to BAP, and the Y-Looped BAP was treated with TL. The Y-Looped BAP formed linear polymers, whereas BAP fused with a C-terminal peptide containing a tyrosine (Y-tag) showed an irregular shape after TL treatment. The sterically confined structure of the Y-Loop could be responsible for the formation of linear BAP polymers. TL-catalyzed copolymerization of Y-Looped BAP and a Y-tagged chimeric antibody-binding protein, pG 2 pA-Y, resulted in the formation of linear bifunctional protein copolymers that could be employed as protein probes in an enzyme-linked immunosorbent assay (ELISA). Copolymers comprising Y-Looped BAP and pG 2 pA-Y at a molar ratio of 100:1 exhibited the highest signal in the ELISA with 26-and 20-fold higher than a genetically fused chimeric protein, BAP-pG 2 pA-Y, and its polymeric form, respectively. This result revealed that the morphology of the copolymers was the most critical feature to improve the functionality of the protein polymers as detection probes, not only for immunoassays but also for other diagnostic applications.

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Use of Multiple Peptide-Based SERS Probes Binding to Different Epitopes on a Protein Biomarker To Improve Detection Sensitivity

Cited by 13 publications

References 33 publications

Ag@Au Core–Shell Porous Nanocages with Outstanding SERS Activity for Highly Sensitive SERS Immunoassay

Ag@Au Core–Shell Porous Nanocages with Outstanding SERS Activity for Highly Sensitive SERS Immunoassay

Ultrasensitive Detection of Low-Abundance Protein Biomarkers by Mass Spectrometry Signal Amplification Assay

Linear Polymerization of Protein by Sterically Controlled Enzymatic Cross-Linking with a Tyrosine-Containing Peptide Loop

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