Method for lowering oxygen affinity of hemoglobin in redcell suspensions, in whole blood and in vivo
US5661182A · kind A · utility
Assignee
Inventors
Key dates
| Filing date | Jun 7, 1995 |
| Grant date | Aug 26, 1997 |
| Priority date | — |
| Expiry date | Jun 7, 2015 |
Classification
- Technology area (CPC C)Chemistry; Metallurgy
- CPC primaryC07C2603/74
- WIPO fieldPharmaceuticals
- WIPO sectorChemistry
Abstract
Drug compounds are used as allosteric modifiers of hemoglobin present in red blood cells. The compounds bind to only a single pair of symmetry related sites in the central water cavity of hemoglobin at the Lys 99.alpha., Arg 141.alpha., and Asn 108 .beta. residues. When one of the drug compounds is bound to hemoglobin, it will join three separate sub-units of the hemoglobin molecule and stabilize the hemoglobin in a lower oxygen affinity state. Because the compounds used in this method are either not bound by serum albumin or only interact to small degrees with serum albumin, the compounds are active in whole blood and in vivo. The process of allosterically modifying hemoglobin towards a low oxygen affinity state in whole blood and in vivo could be used in a wide variety of applications including in treatments for ischemia, heart disease, wound healing, Alzheimer's, depression, schizophrenia, adult respiratory distress syndrome (ARDS), etc., in extending the shelf-life of blood or restoring the oxygen carrying capacity of out-dated blood, and as sensitizers for x-ray irradiation in cancer therapy, as well as in many other applications.
Source: USPTO / EPO open patent data. Objective bibliographic and citation counts.