An efficient expression tag library based on self-assembling amphipathic peptides.

ABSTRACT:

Background

Self-assembling amphipathic peptides (SAPs) may improve protein production or induce the formation of inclusion bodies by fusing them to the N-terminus of proteins. However, they do not function uniformly well with all target enzymes and systematic research on how the composition of SAPs influence the production of fusion protein is still limited.

Results

To improve the efficiency of SAPs, we studied factors that might be involved in SAP-mediated protein production using S1 (AEAEAKAK)₂ as the original SAP and green fluorescent protein (GFP) as the reporter. The results indicate that hydrophobicity and net charges of SAPs play a key role in protein expression. As hydrophobicity regulation tend to cause the formation of insoluble inclusion bodies of prote

SUBMITTER: Zhao W 

PROVIDER: S-EPMC6535861 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature