http://rdf.ncbi.nlm.nih.gov/pubchem/patent/NZ-543111-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_f1144e66b5feb529e22d400c1e870f87 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-47 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P43-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P25-14 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P25-00 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-47 |
| filingDate | 2004-03-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_86f61943ba511e510d211f8c0f391df8 |
| publicationDate | 2007-03-30-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | NZ-543111-A |
| titleOfInvention | Method and use for the reversible aggregation and/or dissociation of polypeptides (comprising peptide repeats derived from prion, such as hexa- or octa-peptides) using a pH dependency mechanism |
| abstract | An alternative method of reversible aggregation and/or dissociation of polypeptides is described. The proteins or polypeptides have an inherent aggregation capability, wherein the aggregation is an oligomerisation of the polypeptide that is based on the presence and the structure of peptide repeats localised in a flexibly disordered domain of this polypeptide. The flexibly disordered domain comprising the peptide repeats is located in close proximity with the N-terminus of the protein amino acid sequence. Preferably, each of the peptide repeats has a sequence that comprises one to four identical octapeptides with the amino acid sequence: PHGGGWGQ. Preferred proteins are selected from the group comprising cellular prion proteins (PrPc) and engineered polypeptides or fusion proteins with a respective inherent reversible aggregation and dissociation capability. Because of the mechanism of aggregation described, the oligomerisation reaction of the protein is reversible in a fluidic environment depending on the pH of this fluidic environment. Oligomerisation occurs at a pH of 6.2 to 7.8, and the dissociation into monomers is reported to be at a pH range of 4.5 to 5.5. Fig 1 shows the primary structure of the human prion protein |
| priorityDate | 2003-03-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 94.