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

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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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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Screening specific polypeptides of breast cancer stem cells from a phage display random peptide library

Oncology Letters ◽

10.3892/ol.2016.5248 ◽

2016 ◽

Vol 12 (6) ◽

pp. 4727-4731 ◽

Cited By ~ 7

Author(s):

Fei Liu ◽

Chun-Ling Qi ◽

Mian Kong ◽

Ting-Ting Liu ◽

Lei Li ◽

...

Keyword(s):

Breast Cancer ◽

Stem Cells ◽

Cancer Stem Cells ◽

Phage Display ◽

Peptide Library ◽

Breast Cancer Stem Cells ◽

Random Peptide Library ◽

Random Peptide

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Novel Zn2+-Chelating Peptides Selected from a Fimbria-Displayed Random Peptide Library

Applied and Environmental Microbiology ◽

10.1128/aem.67.12.5467-5473.2001 ◽

2001 ◽

Vol 67 (12) ◽

pp. 5467-5473 ◽

Cited By ~ 39

Author(s):

Kristian Kjærgaard ◽

Mark A. Schembri ◽

Per Klemm

Keyword(s):

Peptide Library ◽

Carrier Protein ◽

Diverse Range ◽

Binding Peptide ◽

Random Peptide Library ◽

E Coli ◽

Random Peptide ◽

Recombinant Cells ◽

Research Type

ABSTRACT The display of peptide sequences on the surface of bacteria is a technology that offers exciting applications in biotechnology and medical research. Type 1 fimbriae are surface organelles ofEscherichia coli which mediated-mannose-sensitive binding to different host surfaces by virtue of the FimH adhesin. FimH is a component of the fimbrial organelle that can accommodate and display a diverse range of peptide sequences on the E. coli cell surface. In this study we have constructed a random peptide library in FimH. The library, consisting of ∼40 million individual clones, was screened for peptide sequences that conferred on recombinant cells the ability to bind Zn2+. By serial selection, sequences that exhibited various degrees of binding affinity and specificity toward Zn2+were enriched. None of the isolated sequences showed similarity to known Zn2+-binding proteins, indicating that completely novel Zn2+-binding peptide sequences had been isolated. By changing the protein scaffold system, we demonstrated that the Zn2+-binding seems to be uniquely mediated by the peptide insert and to be independent of the sequence of the carrier protein. These findings might be applied in the design of biomatrices for bioremediation purposes or in the development of sensors for detection of heavy metals.

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