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Published on: December 6, 2017
Evolution of disulfide-rich peptide aptamers using cDNA display
1Graduate School of Science and Engineering, Saitama University, Saitama, Japan.
Methods in Molecular Biology (Clifton, N.J.)
|November 19, 2011
Summary
This study details a method using cell-free cDNA display to select disulfide-rich peptide aptamers targeting the interleukin 6 receptor (IL-6R). This technique facilitates disulfide bond shuffling for effective molecular recognition candidate screening.
Area of Science:
- Molecular Biology
- Biochemistry
- Immunology
Background:
- Disulfide-rich protein scaffolds are valuable for molecular recognition.
- cDNA display enables screening of functional peptide aptamers with disulfide bonds.
- Disulfide bond shuffling is key for aptamer discovery.
Purpose of the Study:
- To present a protocol for selecting disulfide-rich peptide aptamers.
- To identify novel aptamers targeting the interleukin 6 receptor (IL-6R).
- To utilize cDNA display for high-throughput aptamer screening.
Main Methods:
- Construction of a 35-amino acid peptide library with a 32-amino acid random region.
- Application of cell-free translation and disulfide bond shuffling.
- Selection of aptamers against IL-6R using cDNA display.
Main Results:
- Successful selection of disulfide-rich peptide aptamers against IL-6R.
- Demonstration of a detailed protocol for aptamer discovery.
- Validation of cDNA display for screening functional aptamers.
Conclusions:
- The presented protocol is effective for identifying specific peptide aptamers.
- Disulfide-rich aptamers offer potential for IL-6R targeting.
- cDNA display is a powerful tool for discovering molecular recognition agents.
