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Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates
Published on: December 6, 2017
[Specific coalescent peptide of CD59 screened by phage library]
1Department of Immunology, Medical College of Qingdao University, Qingdao 266021, China. chengying66@sina.com
Aim:
To screen and identify the short-peptide which specifically bind to human CD59 so as to design short-peptide clamp with counteracting tumor escape activity.
Methods:
Using CHO cells which high express human CD59 as target cells, the phage 12 peptide library was screened for 5 rounds by competitive binding test. After five rounds of screening and competitive binding test, positive phage clones were screened by ELISA and sequenced.
Results:
8 out of 16 phage clones which were chosen randomly were identified to have high binding power to CD59. After sequencing, 3 high homologous amino acids were obtained. DNAstar analysis showed that 3 sequences had some homology with the sequence of human CD2 published by PubMed.
Conclusion:
The obtained sequence HxAxxxxxxPxx is helpful for design of short-peptide clamp of active sites of CD59 related to tumor escape.
Insights
Researchers identified short peptides that bind to human CD59, a protein involved in tumor escape. These peptides can be used to design therapeutic peptide clamps to counteract tumor immune evasion.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- CD59 is a complement regulatory protein that plays a role in tumor immune evasion.
- Targeting CD59 offers a potential strategy to enhance anti-tumor immunity.
Purpose of the Study:
- To screen and identify short peptides that specifically bind to human CD59.
- To design short-peptide clamps with the potential to counteract tumor escape activity.
Main Methods:
- Phage display library screening using Chinese Hamster Ovary (CHO) cells overexpressing human CD59.
- Competitive binding assays, ELISA, and DNA sequencing were employed for clone selection and analysis.
Main Results:
- Eight out of sixteen randomly selected phage clones exhibited high binding affinity to CD59.
- Sequencing revealed three highly homologous amino acid sequences.
- Sequence homology analysis indicated a relationship with human CD2 sequences.
Conclusions:
- The identified peptide sequence (HxAxxxxxxPxx) is valuable for designing short-peptide clamps targeting CD59 active sites.
- This approach holds promise for developing novel therapeutics against tumor immune escape.
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