Pharmaceutical Integrity of Lyophilized Methemoglobin-Albumin Clusters after Reconstitution.

ABSTRACT: Covalent attachment of a ferric hemoglobin (metHb) core to three human serum albumin molecules to form metHb-albumin clusters has previously been used to develop an antidote for hydrogen sulfide poisoning. Lyophilization is one of the most effective approaches to preserve protein pharmaceuticals with minimum contamination and decomposition. However, there is concern that lyophilized proteins may undergo pharmaceutical alteration on reconstitution. This study investigated the pharmaceutical integrity of metHb-albumin clusters on lyophilization and reconstitution with three clinically available reconstitution fluids, (i) sterile water for injection, (ii) 0.9% sodium chloride injection, and (iii) 5% dextrose injection. The metHb-albumin clusters retained their physicochemical properties and s

SUBMITTER: Suzuki Y 

PROVIDER: S-EPMC10308519 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature