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

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.

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Generation of anti-?-amyloid antibodies via phage display technology towards Alzheimer's disease vaccination

Vaccine ◽

10.1016/j.vaccine.2005.01.034 ◽

2005 ◽

Vol 23 (17-18) ◽

pp. 2327-2330 ◽

Cited By ~ 12

Author(s):

B SOLOMON

Keyword(s):

Alzheimer’S Disease ◽

Alzheimer's Disease ◽

Phage Display ◽

Phage Display Technology ◽

Display Technology

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Biotin binders selected from a random peptide library expressed on phage

Biochemical Journal ◽

10.1042/bj2930613 ◽

1993 ◽

Vol 293 (3) ◽

pp. 613-616 ◽

Cited By ~ 37

Author(s):

I Saggio ◽

R Laufer

Keyword(s):

Synthetic Peptide ◽

Peptide Library ◽

Binding Motif ◽

Sequence Motif ◽

Phage Display Technology ◽

Random Peptide Library ◽

Random Peptide ◽

Biotin Binding ◽

Display Technology ◽

Streptavidin Binding

Recombinant biotin-binding phages were affinity-selected from a random peptide library expressed on the surface of filamentous phage. Phage binding to biotinylated proteins was half-maximally inhibited by micromolar concentrations of a monobiotinylated molecule. Sequencing of the peptide inserts of selected phages led to the identification of a previously unknown biotin-binding motif, CXWXPPF(K or R)XXC. A synthetic peptide containing this sequence motif inhibited streptavidin binding to biotinylated BSA with an IC50 of 50 microM. This compound represents the shortest non-avidin biotin-binding peptide identified to date. Our results illustrate that phage display technology can be used to identify novel ligands for a small non-proteinaceous molecule.

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A chitin-oligomer binding peptide obtained by screening of a phage display random peptide library and its affinity modulation corresponding to oxidation–reduction state

Journal of Molecular Catalysis B Enzymatic ◽

10.1016/j.molcatb.2004.02.015 ◽

2004 ◽

Vol 28 (4-6) ◽

pp. 181-184 ◽

Cited By ~ 6

Author(s):

Ei-ichiro Fukusaki ◽

Koichi Ogawa ◽

Atsushi Okazawa ◽

Shin-ichiro Kajiyama ◽

Akio Kobayashi

Keyword(s):

Phage Display ◽

Peptide Library ◽

Binding Peptide ◽

Random Peptide Library ◽

Random Peptide ◽

Oxidation Reduction ◽

Affinity Modulation ◽

Chitin Oligomer

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Three polypeptides screened from phage display random peptide library may be the receptor polypeptide of Mycoplasma genitalium adhesion protein

Microbial Pathogenesis ◽

10.1016/j.micpath.2018.04.058 ◽

2018 ◽

Vol 120 ◽

pp. 140-146 ◽

Cited By ~ 2

Author(s):

Xiangying Deng ◽

Youcong Zhu ◽

Pei Dai ◽

Minjun Yu ◽

Liesong Chen ◽

...

Keyword(s):

Phage Display ◽

Mycoplasma Genitalium ◽

Peptide Library ◽

Adhesion Protein ◽

Random Peptide Library ◽

Random Peptide

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

Molecules ◽

10.3390/molecules26247652 ◽

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.

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