| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_d966dff85e9c2a430558a6266ef1422a |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-90212
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/B82Y5-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/B82Y40-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/B82Y35-00 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-581
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-68
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-26 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-26
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-58
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-68 |
| filingDate |
2019-08-09-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_c3802b85ff40d677f407694c8661a719
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_83e0746d8e7ee2a92a69779e6ecc2e07
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_1426e964ff4f2462eaa2de1e79e1ed63
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_356c6989ea1f7d2af654acf0839b328e
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_9b746e6bc1ada780090ba600098ca510 |
| publicationDate |
2021-10-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
US-2021311066-A1 |
| titleOfInvention |
A metal-reducing enzymatic tag for optical and electron microscopy |
| abstract |
Enzymes that reduce specific metal or metalloid ions to insoluble form are important to science. Peptides isolated from yeast- and phage-display libraries can affect the size and morphology of inorganic materials during their synthesis. Herein, an Se binding peptide was fused to an enzyme capable of reducing selenite (SeO3 2− ) to a Se 0 nanoparticle (SeNP). The fusion of the Se binding peptide to the metalloid reductase provided size control of the resulting SeNP. The SeNP product also remains associated to the enzyme fusion. The Se binding peptide fusion to the enzyme increases the enzyme's SeO3 2− reductase activity. Modification of enzyme activity was absent, and the size control of particles was diminished when the Se binding peptide was added exogenously to the reaction mixture. Binding of the peptide is attributed to His based ligation that results in a conformational change to the peptide. |
| priorityDate |
2018-08-10-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |