scholarly journals Mimotopes for Mycotoxins Diagnosis Based on Random Peptides or Recombinant Antibodies from Phage Library

Molecules ◽  
2021 ◽  
Vol 26 (24) ◽  
pp. 7652
Author(s):  
Wei Sun ◽  
Yan Zhang ◽  
Zhigang Ju
Keyword(s):  
Phage Display ◽  
Recombinant Antibody ◽  
Recombinant Antibodies ◽  
Phage Display Library ◽  
Ease Of Use ◽  
Phage Library ◽  
Phage Display Technology ◽  
Random Peptide ◽  
Display Technology

Mycotoxins, the small size secondary metabolites of fungi, have posed a threat to the safety of medicine, food and public health. Therefore, it is essential to create sensitive and effective determination of mycotoxins. Based on the special affinity between antibody and antigen, immunoassay has been proved to be a powerful technology for the detection of small analytes. However, the tedious preparation and instability of conventional antibodies restrict its application on easy and fast mycotoxins detection. By virtue of simplicity, ease of use, and lower cost, phage display library provides novel choices for antibodies or hapten conjugates, and lead random peptide or recombinant antibody to becoming the promising and environmental friendly immune-reagents in the next generation of immunoassays. This review briefly describes the latest developments on mycotoxins detection using M13 phage display, mainly focusing on the recent applications of phage display technology employed in mycotoxins detection, including the introduction of phage and phage display, the types of phage displayed peptide/recombinant antibody library, random peptides/recombinant antibodies-based immunoassays, as well as simultaneous determination of multiple mycotoxins.

Characterization of 11-dehydro-thromboxane B2 recombinant antibody obtained by phage display technology

2003 ◽  
Vol 68 (4) ◽  
pp. 273-284 ◽  
Author(s):  
Lilian Rumi Tsuruta ◽  
Yoshihisa Tomioka ◽  
Takanori Hishinuma ◽  
Yoshinori Kato ◽  
Kunihiko Itoh ◽  
...  
Keyword(s):  
Phage Display ◽  
Recombinant Antibody ◽  
Thromboxane B2 ◽  
Phage Display Technology ◽  
Display Technology

scholarly journals Epitope Fingerprinting for Recognition of the Polyclonal Serum Autoantibodies of Alzheimer’s Disease

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Luiz Carlos de Oliveira-Júnior ◽  
Fabiana de Almeida Araújo Santos ◽  
Luiz Ricardo Goulart ◽  
Carlos Ueira-Vieira
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Phage Display ◽  
Neural Tissue ◽  
Peptide Library ◽  
Phage Display Technology ◽  
Random Peptide Library ◽  
Random Peptide ◽  
Display Technology ◽  
Polyclonal Serum

Autoantibodies (aAb) associated with Alzheimer’s disease (AD) have not been sufficiently characterized and their exact involvement is undefined. The use of information technology and computerized analysis with phage display technology was used, in the present research, to map the epitope of putative self-antigens in AD patients. A 12-mer random peptide library, displayed on M13 phages, was screened using IgG from AD patients with two repetitions. Seventy-one peptides were isolated; however, only 10 were positive using the Elisa assay technique (Elisa Index > 1). The results showed that the epitope regions of the immunoreactive peptides, identified by phage display analysis, were on the exposed surfaces of the proteins. The putative antigens MAST1, Enah, MAO-A, X11/MINT1, HGF, SNX14, ARHGAP 11A, APC, and CENTG3, which have been associated with AD or have functions in neural tissue, may indicate possible therapeutic targets.

Use of phage display technology for the determination of the targets for small-molecule therapeutics

2010 ◽  
Vol 5 (4) ◽  
pp. 361-389 ◽  
Author(s):  
Yoichi Takakusagi ◽  
Kaori Takakusagi ◽  
Fumio Sugawara ◽  
Kengo Sakaguchi
Keyword(s):  
Phage Display ◽  
Small Molecule ◽  
Phage Display Technology ◽  
Display Technology ◽  
Small Molecule Therapeutics

scholarly journals Citrullination of a phage displayed human peptidome library reveals the fine specificities of rheumatoid arthritis-associated autoantibodies

2021 ◽  
Author(s):  
Gabriel D. Román-Meléndez ◽  
Daniel R. Monaco ◽  
Janelle M. Montagne ◽  
Rachel S. Quizon ◽  
Maximilian F. Konig ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Amino Acid ◽  
Phage Display ◽  
Phage Display Library ◽  
Human Proteome ◽  
Phage Display Technology ◽  
Post Translational Modifications ◽  
Amino Acid Peptide ◽  
Display Technology ◽  
Citrullinated Protein

AbstractPost-translational modifications (PTMs) on proteins can be targeted by antibodies associated with autoimmunity. Despite a growing appreciation for their intrinsic role in disease, there is a lack of highly multiplexed serological assays to characterize the fine specificities of PTM-directed autoantibodies. In this study, we used the programmable phage display technology, Phage ImmunoPrecipitation Sequencing (PhIP-Seq), to profile rheumatoid arthritis (RA) associated anti-citrullinated protein antibody (ACPA) reactivities. Using both an unmodified and peptidylarginine deiminases (PAD)-modified phage display library consisting of ~250,000 overlapping 90 amino acid peptide tiles spanning the human proteome, PTM PhIP-Seq robustly identifies antibodies to citrulline-dependent epitopes. PTM PhIP-Seq was used to quantify key differences among RA patients, including PAD isoform specific ACPA profiles, and thus represents a powerful tool for proteome-scale antibody-binding analyses.

scholarly journals Isolation of a novel Anti-KDR3 Single-chain Variable Fragment Antibody from a Phage Display Library

2019 ◽  
Author(s):  
Shirafkan Kordi ◽  
Mohammad Rahmati-Yamchi ◽  
Mehdi Asghari Vostakolaei ◽  
Ali Etemadie ◽  
Abolfazl Barzegari ◽  
...  
Keyword(s):  
Phage Display ◽  
Growth Factor Receptor ◽  
Phage Display Library ◽  
Vital Role ◽  
Scfv Antibody ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Phage Display Technology ◽  
Display Technology ◽  
Domain 3

Vascular endothelial growth factor receptor 2 (VEGFR-2) is known as one of the important antigens playing a vital role in angiogenesis. In this study, phage display technology (PDT) was used to produce a single-chain variable fragment (scFv) antibody against a region of the domain 3 in VEGFR-2 called kinase insert domain receptor 3 (KDR3). After designing the KDR3 peptide and biopanning, a colony was chosen for scFv antibody expression. Following expression and purification; western blotting, dot blotting and immunofluorescence (IF) were used to evaluate the antibody function. Surface plasmon resonance (SPR) was also employed to measure affinity of produced antibody. Once a colony was selected and transferred to the expression host, the scFv antibody was expressed in the expected range of 28 kDa. Using a designed chromatography column, antibody purification was found to be about 95%. In this study, a novel scFv with the capability of binding to KDR3 was isolated and purified and its intracellular function was investigated and verified.

K-Ras(G12D)-selective inhibitory peptides generated by random peptide T7 phage display technology

2017 ◽  
Vol 484 (3) ◽  
pp. 605-611 ◽  
Author(s):  
Kotaro Sakamoto ◽  
Yusuke Kamada ◽  
Tomoya Sameshima ◽  
Masahiro Yaguchi ◽  
Ayumu Niida ◽  
...  
Keyword(s):  
Phage Display ◽  
Phage Display Technology ◽  
Random Peptide ◽  
Inhibitory Peptides ◽  
Display Technology ◽  
T7 Phage Display ◽  
T7 Phage

scholarly journals generation of hapten-specific recombinant antibodies: antibody phage display technology: a review

2012 ◽  
Vol 50 (No. 6) ◽  
pp. 231-252 ◽  
Author(s):  
J. Brichta ◽  
M. Hnilova ◽  
T. Viskovic
Keyword(s):  
Phage Display ◽  
Recombinant Dna ◽  
Recombinant Antibodies ◽  
Laboratory Animals ◽  
Automatic Process ◽  
Phage Display Technology ◽  
Current Trends ◽  
Antibody Phage ◽  
Antibody Phage Display ◽  
Display Technology

Production of antibodies has been revolutionized by the development of modern molecular biology methods for the expression of recombinant DNA. Phage display technology represents one of the most powerful tools for production and selection of recombinant antibodies and has been recognized as a valuable alternative way for the preparation of antibodies of a desired specificity. In comparison to poly- and monoclonal antibodies, recombinant antibodies using the phage display technology can be prepared faster, in more automatic process and with reduced consumption of laboratory animals. This review summarizes current trends of phage display technology with focus on the generation of hapten-specific recombinant antibodies and gives the examples of successful applications of phage display in the environmental analysis of low molecular weight compound.

scholarly journals Phage display technology for target determination of small-molecule therapeutics: an update

2020 ◽  
Vol 15 (10) ◽  
pp. 1199-1211
Author(s):  
Yoichi Takakusagi ◽  
Kaori Takakusagi ◽  
Kengo Sakaguchi ◽  
Fumio Sugawara
Keyword(s):  
Phage Display ◽  
Small Molecule ◽  
Phage Display Technology ◽  
Display Technology ◽  
Small Molecule Therapeutics ◽  
Target Determination
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