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filingDate 1995-06-07-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 1999-03-30-04:00^^<http://www.w3.org/2001/XMLSchema#date>
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publicationDate 1999-03-30-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber US-5888505-A
titleOfInvention Method for selectively inhibiting the growth of microbes using a haloperoxidase-halide-peroxide system
abstract Haloperoxidases are used to selectively bind to and, in the presence of peroxide and halide, inhibit the growth of target microbes without eliminating desirable microbes or significantly damaging other components, such as host cells, in the environment of the target microbe. When a target microbe, e.g., a pathogenic microbe, has a binding capacity for haloperoxidase greater than that of a desired microbe, e.g., members of the normal flora, the target microbe selectively binds the haloperoxidase with little or no binding of the haloperoxidase by the desired microbe. In the presence of peroxide and halide, the target bound haloperoxidase catalyzes halide oxidation and facilitates the disproportionation of peroxide to singlet molecular oxygen at the surface of the target microbe. The lifetime of singlet molecular oxygen restricts damage to the surface resulting in selective killing of the target microbe with a minimum of collateral damage to the desired microbe or physiological medium. The methods and compositions of the invention are highly useful in the therapeutic or prophylactic antiseptic treatment of human or animal subjects, since their use can be designed to be highly effective in combatting bacterial or fungal infections without significant damage to normal flora or host cells. Suitable haloperoxidases include myeloperoxidase (MPO), eosinophil peroxidase (EPO), lactoperoxidase (LPO), chloroperoxidase (CPO) and derivatives thereof capable of selective binding to target microbes.
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http://rdf.ncbi.nlm.nih.gov/pubchem/substance/SID226395486
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP80878
http://rdf.ncbi.nlm.nih.gov/pubchem/compound/CID9816401
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP04963
http://rdf.ncbi.nlm.nih.gov/pubchem/anatomy/ANATOMYID1591
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCB8AME2
http://rdf.ncbi.nlm.nih.gov/pubchem/substance/SID127796639
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ43206
http://rdf.ncbi.nlm.nih.gov/pubchem/taxonomy/TAXID1306
http://rdf.ncbi.nlm.nih.gov/pubchem/taxonomy/TAXID28037
http://rdf.ncbi.nlm.nih.gov/pubchem/substance/SID419507876
http://rdf.ncbi.nlm.nih.gov/pubchem/compound/CID3641960
http://rdf.ncbi.nlm.nih.gov/pubchem/substance/SID415057377
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP13006
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ8CPD0
http://rdf.ncbi.nlm.nih.gov/pubchem/compound/CID773
http://rdf.ncbi.nlm.nih.gov/pubchem/substance/SID226427933
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ10S82
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP80550
http://rdf.ncbi.nlm.nih.gov/pubchem/substance/SID419523291
http://rdf.ncbi.nlm.nih.gov/pubchem/compound/CID5280450
http://rdf.ncbi.nlm.nih.gov/pubchem/anatomy/ANATOMYID78535
http://rdf.ncbi.nlm.nih.gov/pubchem/substance/SID226409109
http://rdf.ncbi.nlm.nih.gov/pubchem/compound/CID446220
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ2I6W4
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP49290
http://rdf.ncbi.nlm.nih.gov/pubchem/substance/SID419526858
http://rdf.ncbi.nlm.nih.gov/pubchem/compound/CID31388
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCI1S2N3
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCA6ZV70

Total number of triples: 331.