Through the partnership of Myochlor and the University of Illinois, the investigators seek to reduce to practice their previous discovery which enables the generation of novel oxygen transporting therapeutics with augmented functionality. A totally synthetic gene has been constructed which allows the gram level production of human hemoglobin in bacterial hosts. This material, as isolated, incorporates heme and assembles into a functional tetramer. Through genetic modification of this totally synthetic gene , the investigators have produced a novel gene and protein structure which allows fusion of the tetrameric human hemoglobin to a variety of peptide and protein based pharmacologically active compounds. Specifically, they propose to generate a protein conjugate wherein human hemoglobin tetramers are linked through dimerization with the enzyme human superoxide dismutase. The resulting material should display augmented function with regard to oxygen delivery as a blood substitute, due to its increased aggregate size, as well as a novel new functionality of oxygen radical scavenging. The later capacity, delivered as a conjugate with human hemoglobin as a carrier with defined vascular lifetime, should have important clinical effects in preventing reperfusion injury following trauma or myocardial infarct.
Thesaurus Terms: biomaterial development /preparation, blood substitute, drug design /synthesis /production, hemoglobin, oxygen transport, protein engineering, superoxide dismutase biotechnology, chemical conjugate, chimeric protein, drug delivery system, free radical scavenger, genetic manipulation bioengineering /biomedical engineering
