| Literature DB >> 24597567 |
Fantao Meng1, Amy G Tsai, Marcos Intaglietta, Seetharama A Acharya.
Abstract
PEGylation of intramolecularly crosslinked Hb has been studied here to overcome the limitation of dissociation of Hb tetramers. New hexa and deca PEGylated low oxygen affinity PEG-ααHbs have been generated. Influence of PEG conjugation chemistry and the PEG shell structure on the functional properties as well as PEGylation induced plasma expander like properties of the protein has been delineated. The results have established that in the design of PEG-Hbs as oxygen therapeutics, the influence of conjugation chemistry and the PEG shell structure on the oxygen affinity of Hb needs to be optimized independently besides optimizing the PEG shell structure for inducing resuscitation fluid like properties.Entities:
Keywords: PEG shell; PEGylated hemoglobin; PEGylation; blood substitute; oxygen affinity; plasma expander
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Year: 2014 PMID: 24597567 PMCID: PMC4167218 DOI: 10.3109/21691401.2014.885443
Source DB: PubMed Journal: Artif Cells Nanomed Biotechnol ISSN: 2169-1401 Impact factor: 5.678