Phage display based biosensing: Recent advances and challenges

Wang, Mingyang; Pang, Shuang; Zhang, Haohan; Yang, Zhonghuang; Liu, Aihua

doi:10.1016/j.trac.2024.117629

Cited by 12 publications

(2 citation statements)

References 317 publications

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“…Specific biorecognition elements with good affinity are vital in the immunoassay. Phage display is a powerful tool to obtain specific recognition elements of target molecules through biopanning, 20,21 which provides more options for the construction of biosensors. 22 Compared with traditional antibodies, M13 phage-screened peptides have several advantages: (1) The major capsid protein (pVIII) of the phage serves as a scaffold, which can be recognized by thousands of M13 phage antibodyconjugated horseradish peroxidase (HRP) (anti-M13-HRP), helping to enhance signaling.…”

Section: ■ Introductionmentioning

confidence: 99%

Sensitive Dual-Signal ELISA Based on Specific Phage-Displayed Double Peptide Probes with Internal Filtering Effect to Assay Monkeypox Virus Antigen

Pang,

Wang,

Yuan

et al. 2024

Anal. Chem.

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The global spread of monkeypox has become a worldwide public healthcare issue. Therefore, there is an urgent need for accurate and sensitive detection methods to effectively control its spreading. Herein, we screened by phage display two peptides M4 (sequence: DPCGERICSIAL) and M6 (sequence: SCSSFLCSLKVG) with good affinity and specificity to monkeypox virus (MPXV) B21R protein. To simulate the state of the peptide in the phage and to avoid spatial obstacles of the peptide, GGGSK was added at the C terminus of M4 and named as M4a. Molecular docking shows that peptide M4a and peptide M6 are bound to different epitopes of B21R by hydrogen bonds and salt-bridge interactions, respectively. Then, peptide M4a was selected as the capture probe, phage M6 as the detection probe, and carbonized polymer dots (CPDs) as the fluorescent probe, and a colorimetric and fluorescent double-signal capture peptide/antigen/signal peptidedisplayed phage sandwich ELISA triggered by horseradish peroxidase (HRP) through a simple internal filtration effect (IFE) was constructed. HRP catalyzes H 2 O 2 to oxidize 3,3′,5,5′-tetramethylbenzidine (TMB) to generate blue oxidized TMB, which can further quench the fluorescence of CPDs through IFE, enabling to detect MPXV B21R in colorimetric and fluorescent modes. The proposed simple immunoassay platform shows good sensitivity and reliability in MPXV B21R detection. The limit of detection for colorimetric and fluorescent modes was 27.8 and 9.14 pg/mL MPXV B21R, respectively. Thus, the established double-peptide sandwich-based dual-signal immunoassay provides guidance for the development of reliable and sensitive antigen detection capable of mutual confirmation, which also has great potential for exploring various analytical strategies for other respiratory virus surveillance.

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Section: ■ Introductionmentioning

confidence: 99%

Sensitive Dual-Signal ELISA Based on Specific Phage-Displayed Double Peptide Probes with Internal Filtering Effect to Assay Monkeypox Virus Antigen

Pang,

Wang,

Yuan

et al. 2024

Anal. Chem.

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“…Soon after its birth in 1985, following a short lag period [ 1 , 2 ], the phage display technology enjoyed a tremendous exponential growth, demonstrating its competence and performance in solving numerous challenging problems in material science, bioengineering, and medicine, including cancer research [ 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 ] ( Figure 1 ). This Special Issue aims to illustrate the promise of phage display as a universal research tool in cancer research.…”

Section: Introductionmentioning

confidence: 99%

Phage Display in Cancer Research: Special Issue Editorial

Petrenko

2024

Viruses

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Identification of Peptide Binding Motifs for Calcium Sulfate Hemihydrate using Phage Display

Madeja,

Wilke,

Scheck

et al. 2024

Chemistry A European J

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Selective control over crystallization in complex multicomponent systems such as hydrating cements is a key issue in modern material science. In this context, rational selection‐based approaches appear highly promising in the quest for new additive chemistries. Here we have used phage display to identify peptide structures showing high affinity to adsorb on the surfaces of calcium sulfate hemihydrate (also referred to as bassanite), an important hydraulic binder employed in large scales by the construction industry. The results suggest a triplet of amino acids consisting of aspartic acid, serine and leucine, to maintain strong interactions with the surfaces of hemihydrate particles. This notion is confirmed by actual hydration experiments, in which the identified peptide motif provides strictly selective effects during the transformation of bassanite into more stable gypsum. Our work thus contributes to a better understanding of hydraulic binders and their required improvement for a sustainable future.

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Phage display based biosensing: Recent advances and challenges

Cited by 12 publications

References 317 publications

Sensitive Dual-Signal ELISA Based on Specific Phage-Displayed Double Peptide Probes with Internal Filtering Effect to Assay Monkeypox Virus Antigen

Sensitive Dual-Signal ELISA Based on Specific Phage-Displayed Double Peptide Probes with Internal Filtering Effect to Assay Monkeypox Virus Antigen

Phage Display in Cancer Research: Special Issue Editorial

Identification of Peptide Binding Motifs for Calcium Sulfate Hemihydrate using Phage Display

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