Neuroblastoma tumor cell-binding peptides identified through random peptide phage display

2001 ◽  
Vol 171 (2) ◽  
pp. 153-164 ◽  
Author(s):  
Jianbing Zhang ◽  
Herbert Spring ◽  
Manfred Schwab
Keyword(s):  
Tumor Cell ◽  
Phage Display ◽  
Cell Binding ◽  
Random Peptide ◽  
Neuroblastoma Tumor ◽  
Peptide Phage Display ◽  
Binding Peptides

Screening and Identification of PLK1-Polo Box Binding Peptides by High-Throughput Sequencing of Phage-Selected Libraries

2019 ◽  
Vol 26 (8) ◽  
pp. 620-633 ◽  
Author(s):  
Nousheen Bibi ◽  
Hafsa Niaz ◽  
Ted Hupp ◽  
Mohammad Amjad Kamal ◽  
Sajid Rashid
Keyword(s):  
Next Generation Sequencing ◽  
Phage Display ◽  
High Throughput ◽  
High Throughput Sequencing ◽  
B Lymphocyte ◽  
Fluorescent Protein ◽  
Next Generation ◽  
Peptide Phage Display ◽  
Binding Peptides ◽  
Generation Sequencing

Background: Human proteome contains a plethora of short linear peptide motifs that is crucial for signaling and other cellular processes. These motifs are difficult to identify due to lack of systematic approach for their detection. Objective: Here we demonstrate the use of peptide phage display in combination with high throughput next generation sequencing to identify enriched peptide sequences through biopanning process against polo box domain (PBD) of mitotic polo like kinase 1 (Plk1). Methods: Purified recombinant Plk1 and two unrelated controls namely B-lymphocyte antigen (CD20) and fluorescent protein (mCherry) were subjected to peptide phage display analysis. Bacterially-propagated phage DNA was amplified by PCR using triplet bar coded primers to tag the pool from each amplicon. Results: Proteomic peptide phage display along with next generation sequencing and Bioinformatics analysis demonstrated several known and putative novel interactions which were potentially related to Plk1-PBD. With our strategy, we were able to identify and characterize several Plk1-PBD binding peptides, as well as define more precisely, consensus sequences. Conclusion: We believe that this information could provide valuable tools for exploring novel interaction involved in Plk1 signaling as well as to choose peptides for Plk1 specific drug development.

Mimotopes for lupus-derived anti-DNA and nucleosome-specific autoantibodies selected from random peptide phage display libraries: facts and follies

2005 ◽  
Vol 296 (1-2) ◽  
pp. 83-93 ◽  
Author(s):  
Jürgen W. Dieker ◽  
Yong-Jiang Sun ◽  
Cor W. Jacobs ◽  
Chaim Putterman ◽  
Marc Monestier ◽  
...  
Keyword(s):  
Phage Display ◽  
Random Peptide ◽  
Phage Display Libraries ◽  
Peptide Phage Display

Application of Random Peptide Phage Display to the Study of Nuclear Hormone Receptors

2003 ◽  
pp. 118-142 ◽  
Author(s):  
Ching-yi Chang ◽  
John D Norris ◽  
Michelle Jansen ◽  
Huey-Jing Huang ◽  
Donald P McDonnell
Keyword(s):  
Phage Display ◽  
Hormone Receptors ◽  
Nuclear Hormone Receptors ◽  
Random Peptide ◽  
Peptide Phage Display

scholarly journals Synthetic Peptides as Potential Antigens for Cutaneous Leishmaniosis Diagnosis

2017 ◽  
Vol 2017 ◽  
pp. 1-10 ◽  
Author(s):  
Juliana Seger Link ◽  
Silvana Maria Alban ◽  
Carlos Ricardo Soccol ◽  
Gilberto Vinicius Melo Pereira ◽  
Vanete Thomaz Soccol
Keyword(s):  
Phage Display ◽  
Synthetic Peptides ◽  
Leishmania Braziliensis ◽  
Protein Databases ◽  
Random Peptide ◽  
Fmoc Chemistry ◽  
Phage Display Libraries ◽  
Incomplete Freund’S Adjuvant ◽  
Peptide Phage Display ◽  
Cutaneous Leishmaniosis

This work’s goal was to research new candidate antigens for cutaneous leishmaniosis (CL). In order to reach the goal, we used random peptide phage display libraries screened using antibodies fromLeishmania braziliensispatients. After selection, three peptides (P1, P2, and P3) were synthesized using Fmoc chemistry. The peptides individually or a mixture of them (MIX) was subsequently emulsified in complete and incomplete Freund’s adjuvant and injected subcutaneously in golden hamsters. Sera from the hamsters administered with P1 presented antibodies that recognized proteins between 76 and 150 kDa fromL. braziliensis. Sera from hamsters which had peptides P2 and P3, as well as the MIX, administered presented antibodies that recognized proteins between 52 and 76 kDa ofL. braziliensis. The research on the similarity of the peptides’ sequences in protein databases showed that they match a 63 kDa glycoprotein. The three peptides and the MIX were recognized by the sera from CL patients by immunoassay approach (ELISA). The peptides’ MIX showed the best performance (79% sensitivity) followed by the P1 (72% sensitivity), and the AS presented 91% sensitivity. These results show a new route for discovering molecules for diagnosis or for immunoprotection against leishmaniosis.

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