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Abstract
Hemoglobin (Hb) derivatization for blood substitute purposes often involves multi-step processes including redox reagents such as borohydride and periodate, with possible subsequent side effects. Disuccinimidyl suberate (DSS) allows protein cross-linking without toxic side-products, forming one-step peptide bonds with the lysine residues. Here, we report that Hb polymers were obtained using DSS, making this the first report of a single-step polymerization for blood substitutes. The increase in autooxidation rate incurred by this polymerization is completely reversed when BSA is copolymerized with Hb. Copolymerization of Hb with BSA appears to be beneficial for alleviating pro-oxidant effects, regardless of the polymerizing agent employed.
Acknowledgements
OZ thanks the “Babes-Bolyai” University for a research scholarship.
Declaration of interest
The authors report no declarations of interest. The authors alone are responsible for the content and writing of the paper.
The work shown here has been supported by the Romanian Ministry for Education and Research (grant PCCE 140/2008) and by a PhD scholarship to FS (Contract POSDRU/88/1.5/S/60185 – “Innovative doctoral studies in a knowledge based society”).