http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2009234096-A1

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classificationCPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N2760-16122
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classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-005
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K7-06
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filingDate 2009-02-17^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0edd1fb8f9e203c9dc8192fbaa2d9a8f
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_67ec63002ab58f34e9f09162c106d9a6
publicationDate 2009-09-17^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber US-2009234096-A1
titleOfInvention Influenza inhibiting compositions and methods
abstract The present invention provides compositions useful for treating or preventing influenza infections. The composition comprises an isolated polypeptide including a sequence of at least 8 contiguous amino acid residues of the fusion initiation region (FIR) of an influenza hemagglutinin 2 protein or a peptide analog of the sequence. The FIR is a segment of the full length hemagglutinin 2 protein which is bounded by an amino-terminal region within the amino-terminal alpha-helix thereof and a carboxy terminus within the carboxy-terminal alpha-helix thereof, with a cysteine loop therebetween. The amino-terminal region of the FIR comprises a portion of the final 10 to 20 amino acid residues of the amino-terminal alpha-helix of the hemagglutinin 2 protein, and includes 3 or 4 hydrophobic amino acid residues, a positively-charged amino acid residue, a negatively-charged amino acid residue, and an aromatic amino acid residue. The carboxy terminus of the FIR is the carboxy terminus of the first peptide sequence of the hemagglutinin 2 protein beyond the amino terminal helix, which exhibits a positive Wimley-White interfacial hydrophobicity.
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