High-affinity phage-displayed peptide as a recognition probe for the detection of Cry2Ad2-3

Wang, Yun; Zhang, Xiao; Xie, Yajing; Wu, Aihua; Zai, Xueming; Liu, Xianjin

doi:10.1016/j.ijbiomac.2019.06.164

Cited by 6 publications

(3 citation statements)

References 29 publications

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“…One of the most significant observation is that the interaction of the Pep2856-PPG was 9-fold stronger than Pep2856-sAP, presumably because the positive charge of Pep2856 (+4) increases the electrostatic interaction with the negative groups in the PPG molecule at sites different to the active site. These affinity values are like the K D values of high-affinity antibodies, generally considered to be in the range of 1 to 10 −3 nM [ 38 ]. Our results demonstrated than the affinity values are similar to the K D values reported by other research where many peptide-based protein ligands, called synbodies, have high affinity and with a K D < 5 nM [ 39 , 40 ].…”

Section: Results and Analysismentioning

confidence: 99%

Design and characterization of high-affinity synthetic peptides as bioreceptors for diagnosis of cutaneous leishmaniasis

et al. 2021

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Cutaneous leishmaniasis (CL) is one of the illnesses caused by Leishmania parasite infection, which can be asymptomatic or severe according to the infecting Leishmania strain. CL is commonly diagnosed by directly detecting the parasites or their DNA in tissue samples. New diagnostic methodologies target specific proteins (biomarkers) secreted by the parasite during the infection process. However, specific bioreceptors for the in vivo or in vitro detection of these novel biomarkers are rather limited in terms of sensitivity and specificity. For this reason, we here introduce three novel peptides as bioreceptors for the highly sensitive and selective identification of acid phosphatase (sAP) and proteophosphoglycan (PPG), which have a crucial role in leishmaniasis infection. These high-affinity peptides have been designed from the conservative domains of the lectin family, holding the ability to interact with the biological target and produce the same effect than the original protein. The synthetic peptides have been characterized and the affinity and kinetic constants for their interaction with the targets (sAP and PPG) have been determined by a surface plasmon resonance biosensor. Values obtained for K D are in the nanomolar range, which is comparable to high-affinity antibodies, with the additional advantage of a high biochemical stability and simpler production. Pep2854 exhibited a high affinity for sAP (K D = 1.48 nM) while Pep2856 had a good affinity for PPG (K D 1.76 nM). This study evidences that these peptidomimetics represent a novel alternative tool to the use of high molecular weight proteins for biorecognition in the diagnostic test and biosensor devices for CL.

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Section: Results and Analysismentioning

confidence: 99%

Design and characterization of high-affinity synthetic peptides as bioreceptors for diagnosis of cutaneous leishmaniasis

et al. 2021

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“…Cry2Aa and Cry2Ab have also been successfully incorporated with Cry1A to delay insect resistance in plants (Qiu et al., 2017). The sensitive detection of Cry2A toxin in food and the environment is necessary to supervise biopesticides (Wang et al., 2019). Pep5, a peptide displayed by recombinant phage M13 with a sequence of ACSYNHNSKCGGG exhibits high specificity and sensitivity to Cry2Ad2‐3, with low cross‐reactivity to other Cry toxins.…”

Section: Immunochemiluminescence Techniques For Detection Of Microbia...mentioning

confidence: 99%

Phage‐based technologies for highly sensitive luminescent detection of foodborne pathogens and microbial toxins: A review

Guo

et al. 2022

Comp Rev Food Sci Food Safe

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Foodborne pathogens and microbial toxins are the main causes of foodborne illness. However, trace pathogens and toxins in foods are difficult to detect. Thus, techniques for their rapid and sensitive identification and quantification are urgently needed. Phages can specifically recognize and adhere to certain species of microbes or toxins due to molecular complementation between capsid proteins of phages and receptors on the host cell wall or toxins, and thus they have been successfully developed into a detection platform for pathogens and toxins. This review presents an update on phage‐based luminescent detection technologies as well as their working principles and characteristics. Based on phage display techniques of temperate phages, reporter gene detection assays have been designed to sensitively detect trace pathogens by luminous intensity. By the host‐specific lytic effects of virulent phages, enzyme‐catalyzed chemiluminescent detection technologies for pathogens have been exploited. Notably, these phage‐based luminescent detection technologies can discriminate viable versus dead microbes. Further, highly selective and sensitive immune‐based assays have been developed to detect trace toxins qualitatively and quantitatively via antibody analogs displayed by phages, such as phage‐ELISA (enzyme‐linked immunosorbent assay) and phage‐IPCR (immuno‐polymerase chain reaction). This literature research may lead to novel and innocuous phage‐based rapid detection technologies to ensure food safety.

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“…Among them, the most frequently used format is double-antibody sandwich ELISAs (DAS-ELISAs), which generally depend on the traditional polyclonal antibodies (PAbs) and monoclonal antibodies (MAbs) [ 17 , 18 ]. Besides, genetically engineered antibodies (e.g., ScFvs) and phage-displayed peptides have been applied in DAS-ELISA for Cry toxin analysis [ 19 , 20 ]. However, ScFvs and peptides usually exhibited relatively low affinity and poor stability [ 21 , 22 ].…”

Section: Introductionmentioning

confidence: 99%

Quantum-Dot-Bead-Based Fluorescence-Linked Immunosorbent Assay for Sensitive Detection of Cry2A Toxin in Cereals Using Nanobodies

Qiu

You

et al. 2022

Foods

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In this study, a quantum-dot-bead (QB)-based fluorescence-linked immunosorbent assay (FLISA) using nanobodies was established for sensitive determination of the Cry2A toxin in cereal. QBs were used as the fluorescent probe and conjugated with a Cry2A polyclonal antibody. An anti-Cry2A nanobody P2 was expressed and used as the capture antibody. The results revealed that the low detection limit of the developed QB-FLISA was 0.41 ng/mL, which had a 19-times higher sensitivity than the traditional colorimetric ELISA. The proposed assay exhibited a high specificity for the Cry2A toxin, and it had no evident cross-reactions with other Cry toxins. The recoveries of Cry2A from the spiked cereal sample ranged from 86.6–117.3%, with a coefficient of variation lower than 9%. Moreover, sample analysis results of the QB-FLISA and commercial ELISA kit correlated well with each other. These results indicated that the developed QB-FLISA provides a potential approach for the sensitive determination of the Cry2A toxin in cereals.

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High-affinity phage-displayed peptide as a recognition probe for the detection of Cry2Ad2-3

Cited by 6 publications

References 29 publications

Design and characterization of high-affinity synthetic peptides as bioreceptors for diagnosis of cutaneous leishmaniasis

Design and characterization of high-affinity synthetic peptides as bioreceptors for diagnosis of cutaneous leishmaniasis

Phage‐based technologies for highly sensitive luminescent detection of foodborne pathogens and microbial toxins: A review

Quantum-Dot-Bead-Based Fluorescence-Linked Immunosorbent Assay for Sensitive Detection of Cry2A Toxin in Cereals Using Nanobodies

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