Functional recombinant apolipoprotein A5 that is stable at high concentrations at physiological pH.

ABSTRACT: APOA5 is a low-abundance exchangeable apolipoprotein that plays critical roles in human triglyceride (TG) metabolism. Indeed, aberrations in the plasma concentration or structure of APOA5 are linked to hypertriglyceridemia, hyperchylomicronemia, myocardial infarction risk, obesity, and coronary artery disease. While it has been successfully produced at low yield in bacteria, the resulting protein had limitations for structure-function studies due to its low solubility under physiological buffer conditions. We hypothesized that the yield and solubility of recombinant APOA5 could be increased by: i) engineering a fusion protein construct in a codon optimized expression vector, ii) optimizing an efficient refolding protocol, and iii) screening buffer systems at physiologi

SUBMITTER: Castleberry M 

PROVIDER: S-EPMC6997596 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature