Antibody-free and selective detection of okadaic acid using an affinity peptide-based indirect assay

Cho, Chae Hwan; Park, Chan Yeong; Chun, Hyang Sook; Park, Tae Jung; Park, Jong Pil

doi:10.1016/j.foodchem.2023.136243

Cited by 14 publications

(3 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Phage display technology employs phages as carriers for presenting foreign proteins or peptides . The advances in phage display technology expand the diversity of peptide recognition molecules for biosensors and hold a crucial role in biodetection . M13 bacteriophage exhibits broad temperature and pH stability, which offers the benefits of cost-effective amplification and easy manipulation.…”

Section: Introductionmentioning

confidence: 99%

Lateral Flow Immunochromatographic Assay for Competitive Detection of Crustacean Allergen Tropomyosin Using Phage-Displayed Shark Single-Domain Antibody

Jiao,

Xie,

et al. 2024

J. Agric. Food Chem.

View full text Add to dashboard Cite

The common food allergy crustacean tropomyosin (TM) poses a significant food safety challenge, which requires rapid and sensitive methods for screening TM in food. Herein, the variable new antigen receptor (VNAR) single-domain antibodies specific for the crustacean TM were isolated from a nai ̈ve phage-displayed shark VNAR library. Subsequently, a lateral flow immunochromatographic assay (LFIA) based on the gold nanoparticle-labeled phage-displayed shark VNAR (AuNPs@PSV) probe was developed for the detection of TM in food. The AuNPs@PSV-LFIA took 15 min for one test and had a visual limit of detection (vLOD) of 0.1 μg/mL and an instrumental LOD of 0.02 μg/mL. Good selectivity, accuracy, precision, and stability were confirmed for the AuNPs@PSV-LFIA. Moreover, the test results of 21 commercially available food products consisted of the allergen labels and were validated by a commercial ELISA kit. Therefore, this work demonstrated the great potential of VNAR for detecting TM in food by LFIA.

show abstract

Section: Introductionmentioning

confidence: 99%

Lateral Flow Immunochromatographic Assay for Competitive Detection of Crustacean Allergen Tropomyosin Using Phage-Displayed Shark Single-Domain Antibody

Jiao,

Xie,

et al. 2024

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…[15] In another study, researchers developed an affinity peptide-based direct competition enzyme-linked immunosorbent assay (dc-ELISA) for the detection of Okadaic acid (OA) in seafood. [16] Kim at al., developed a novel sensor that utilizes affinity peptide-immobilized hydrogel microspheres for the selective detection of influenza A virus (IAV) H3N2, achieving quantitative detection. [17] Shi et al employed biopanning approaches to select specific peptides against immobilized histamine hapten, aiming to develop a fluorescence detection platform for histamine sensing.…”

Section: Introductionmentioning

confidence: 99%

Peptide‐Based Recognition Agents of Histamine: A Biopanning Approach with Enhanced Specificity

Öz,

Dudak

2024

ChemBioChem

View full text Add to dashboard Cite

Histamine is a biogenic amine that poses a potential threat to public health due to its toxicological effects. In this study, we identified histamine‐binding peptides by screening a random 12‐mer peptide library, employing a novel biopanning approach that excluded histidine‐binding sequences in the final round. This additional step enhanced the selectivity of the peptides and prevented interference from histidine during detection. The binding affinities of synthesized peptides to histamine were assessed using isothermal titration calorimetry (ITC). Among the identified peptides, HBF10 (SGFRDGIEDFLW) and HBF26 (IPLENQHKIYST) showed significant affinity to histamine, with Kavalues of 2.56×104 (M‐1) and 8.94×104 (M‐1), respectively. Notably, the identified peptides did not demonstrate binding affinity towards histidine, despite its structural similarity to histamine. Subsequently, the surface plasmon resonance (SPR) sensor surface was prepared by immobilizing the peptide HBF26 to investigate the potential of the peptide as a recognition agent for histamine detection. The findings suggest that the identified peptides have an affinity to histamine specifically, showcasing their potential applications as diagnostic agents with specific targeting capabilities.

show abstract

“…Currently, cutting-edge sensor platforms, including surfaced-enhanced Raman scattering (SERS), electrochemical (EC) sensor systems, and fluorescence sensor systems, have emerged as powerful and promising tools. − These methods have shown their efficacy in achieving sensitive and convenient detection of influenza virus by employing various bioreceptors such as antibodies, aptamers, and peptides as recognition elements. Among the bioreceptors, peptides have emerged as a particularly promising choice by playing an important role in detecting numerous biological and chemical molecules, including viruses, food allergy, disease biomarkers, and small molecules, in recent years. − Furthermore, peptides can be chemically synthesized with ease, allowing modifications that enhance stability, binding affinity, and specificity to overcome the disadvantages of antibodies such as complex production and fragility in harsh environments.…”

Section: Introductionmentioning

confidence: 99%

Affinity Peptide-Tethered Suspension Hydrogel Sensor for Selective and Sensitive Detection of Influenza Virus

Kim,

Jeong,

Hwang

et al. 2023

ACS Appl. Mater. Interfaces

Self Cite

View full text Add to dashboard Cite

Influenza viruses are known to cause pandemic flu outbreaks through both inter-human and animal-to-human transmissions. Therefore, the rapid and accurate detection of such pathogenic viruses is crucial for effective pandemic control. Here, we introduce a novel sensor based on affinity peptide-immobilized hydrogel microspheres for the selective detection of influenza A virus (IAV) H3N2. To enhance the binding affinity performance, we identified novel affinity peptides using phage display and further optimized their design. The functional hydrogel microspheres were constructed using the drop microfluidic technique, employing a structure composed of natural (chitosan) and synthetic (poly(ethylene glycol) diacrylate and PEG 6 kDa) polymers with the activation of azadibenzocyclooctyne for the subsequent click chemistry reaction. The binding peptide-immobilized hydrogel microsphere (BP-Hyd) was characterized by field emission scanning electron microscopy, X-ray photoelectron spectroscopy, and Fourier transform infrared spectroscopy and exhibited selective detection capability for the IAV H3N2. To capture the detected IAV H3N2, a Cy3-labeled IAV hemagglutinin antibody was utilized. By incorporating the affinity peptide with hydrogel microspheres, we achieved quantitative and selective detection of IAV H3N2 with a detection limit of 1.887 PFU mL–1. Furthermore, the developed suspension sensor exhibited excellent reproducibility and showed reusability potential. Our results revealed that the BP-Hyd-based fluorescence sensor platform could be feasibly employed to detect other pathogens because the virus-binding peptides can be easily replaced with other peptides through phage display, enabling selective and sensitive binding to different targets.

show abstract

Antibody-free and selective detection of okadaic acid using an affinity peptide-based indirect assay

Cited by 14 publications

References 35 publications

Lateral Flow Immunochromatographic Assay for Competitive Detection of Crustacean Allergen Tropomyosin Using Phage-Displayed Shark Single-Domain Antibody

Lateral Flow Immunochromatographic Assay for Competitive Detection of Crustacean Allergen Tropomyosin Using Phage-Displayed Shark Single-Domain Antibody

Peptide‐Based Recognition Agents of Histamine: A Biopanning Approach with Enhanced Specificity

Affinity Peptide-Tethered Suspension Hydrogel Sensor for Selective and Sensitive Detection of Influenza Virus

Contact Info

Product

Resources

About