Protein scaffolds containing some disulfide bonds (e.g., Knottin, Kunitz domain, etc.) are promising candidates for molecular recognition. cDNA display has been developed to screen functional disulfide-rich peptide aptamers from a vast library by promoting disulfide bond shuffling after the synthesis of peptides in a cell-free translation system. Here we present a detailed protocol for the selection of disulfide-rich peptide aptamers against interleukin 6 receptor (IL-6R) from a 35-amino acid peptide library containing 32 amino acids in the random region, which is linked to its genotype by cDNA display. © 2012 Springer Science+Business Media, LLC.
CITATION STYLE
Mochizuki, Y., & Nemoto, N. (2012). Evolution of disulfide-rich peptide aptamers using cdna display. Methods in Molecular Biology, 805, 237–250. https://doi.org/10.1007/978-1-61779-379-0_13
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