http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2007084507-A2

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http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_f8c0982b0f02b1ed6d20a315370a3a3a
classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K9-008
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classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-14
filingDate 2007-01-16-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_869477829d8050d56f579e1658d1728a
publicationDate 2007-07-26-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber WO-2007084507-A2
titleOfInvention [ψ[CH2NH]PG4] GLYCOPEPTIDE ANTIBIOTIC ANALOGS
abstract [ψ[CH2NH]PG4] glycopeptide antibiotic analogs are reengineered forms of glycopeptides that exhibit antimicrobial activity against both wild type and glycopeptide antibiotic resistant strains of microorganisms. For example, [Ψ[CH2NH]Tpg4] vancomycin aglycon is a reengineered form of vancomycin that exhibits antimicrobial activity (MIC = 31 µg/mL) against both wild type and VanA resistant organism (E. faecalis BM4166). The VanA resistant organism achieves its resistance, upon glycopeptide antibiotic challenge, by remodeling its D-Ala-D-Ala peptidoglycan cell wall precursor to D-Ala-D-Lac. [ψ[CH2NH]PG4] glycopeptide antibiotic analogs have an altered glycopeptide backbone wherein the carbonyl of the fourth amino acid residue of the glycopeptide backbone has been replaced with a methylene. This alteration of the glycopeptide backbone imparts dual binding affinities for both D-Ala-D-Ala and D-Ala-D-Lac and dual antimicrobial activities for both wild type and resistant strains. For example, [Ψ[CH2NH]Tpg4]vancomycin aglycon displays a antimicrobial potency that reflects its altered binding characteristics.
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priorityDate 2006-01-13-04:00^^<http://www.w3.org/2001/XMLSchema#date>
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