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classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-15
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-50
filingDate 2019-07-12-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_a8f0cc28e884d6bb81c67b4404579145
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0d350d3abf9391a2ee6d5388258139cc
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e14c4f6f687ad0cc3628a48f2c5d95c5
publicationDate 2020-01-16-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber JP-2020007309-A
titleOfInvention Method for producing chemically cross-linked peptide, chemically cross-linked peptide prepared using the method, and peptide library constructed by using the peptide by cDNA display method
abstract The present invention provides a chemically crosslinked peptide having a stable structure under reducing conditions. An mRNA is prepared by transcription from a DNA having a desired sequence, and the mRNA is ligated to an mRNA binding site of a linker having a peptide binding site, a solid phase binding site and an mRNA binding site to prepare a linker, The linker is translated by a cell-free translation system, and a peptide corresponding to the mRNA is synthesized in a state of being bound to a peptide binding site of the linker, and the peptide-bonded linker is immobilized on a solid phase, and immobilized on the solid phase. By reducing the S—S bond in the peptide bonded to the linker thus formed by reduction, and then bonding the selected divalent cross-linking compound that forms a cross-link with the reduced —SH group A chemically cross-linked peptide having a cross-linking efficiency of at least 90% with a linker by gel shift assay in which an intramolecular cross-link has been formed. [Selection diagram] None
isCitedBy http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2021148870-A1
priorityDate 2019-07-12-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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