Lyophilized annelid mega-hemoglobin retains its' quaternary structure and oxygen equilibrium properties after room temperature storage for over 6 months.

ABSTRACT: The long-term storage stability and portability of hemoglobin (Hb)-based oxygen carriers are important design criteria in the development of these therapeutics. Lyophilization or storing proteins in a freeze-dried form is known to increase storage lifetime and reduce overall weight. In this study, we lyophilized the extracellular mega-hemoglobin of the annelid Lumbricus terrestris and tested the storage stability at different temperatures and oxygenation conditions. Storage in refrigerated conditions for over 6 months in the presence of N2 reduced oxidation by 50% while storage at room temperature in the presence of N2 reduced oxidation by 60%, all while maintaining the structural stability of the mega-hemoglobin. We also demonstrated a reliable strategy to freeze dry Hbs in the presence o

SUBMITTER: Savla C 

PROVIDER: S-EPMC8853537 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature