title: Evolution of disulfide-rich peptide aptamers using cDNA display.
abstract: 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.
authors.affiliation: Graduate School of Science and Engineering, Saitama University, Saitama, Japan.
authors.forename: Yuki
authors.initials: Y
authors.lastname: Mochizuki
authors.forename: Naoto
authors.initials: N
authors.lastname: Nemoto
mesh_terms: D052158:Aptamers, Peptide / Q000138:chemical synthesis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018076:DNA, Complementary / Q000235:genetics*; D019020:Directed Molecular Evolution; D004220:Disulfides / Q000737:chemistry*; D019151:Peptide Library
chemical_list: D052158:Aptamers, Peptide; D018076:DNA, Complementary; D004220:Disulfides; D019151:Peptide Library