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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_59c6a921f33fe0adc58c2b6177184515
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_b3127c0ebee3f865b211b019fac84286
classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07C237-22
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filingDate 2016-10-24-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2018-06-19-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f609faf99e0f04e4f6c5cc469df78ac4
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_4ed90a280de0a126cc9187d5efed46af
publicationDate 2018-06-19-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber US-10000531-B2
titleOfInvention Gamma-AA-peptide STAT3/DNA inhibitors and methods of use
abstract STAT3 hyperphosphorylation, dimerization and DNA binding are required for its ability to contribute to malignant transformation. As such, STAT3 has been recognized as a promising target for cancer therapy. Although a number of inhibitors of STAT3-STAT3 dimerization have been reported, molecular ligands that prevent interactions between STAT3 and DNA are very rare. The γ-AApeptide-based one-bead-one-compound (OBOC) combinatorial library was used, and identified γ-AApeptides that can selectively inhibit STAT3/DNA interaction and suppress the expression levels of STAT3 target genes in intact cells. The results not only validate γ-AApeptides as novel inhibitors of STAT3 signaling pathway, but also demonstrate that in addition to the SH2 domain, the DNA binding domain of STAT3 is targetable for the development of new generation of anti-cancer therapeutics. This also validates the approach of OBOC combinatorial library for the identification of ligands targeting traditionally recognized “undruggable targets”.
priorityDate 2014-04-25-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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