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ABSTRACT: Background
Recombinant protein expression in bacteria often leads to the formation of intracellular insoluble protein deposits, a major bottleneck for the production of soluble and active products. However, in recent years, these bacterial protein aggregates, commonly known as inclusion bodies (IBs), have been shown to be a source of stable and active protein for biotechnological and biomedical applications. The formation of these functional IBs is usually facilitated by the fusion of aggregation-prone peptides or proteins to the protein of interest, leading to the formation of amyloid-like nanostructures, where the functional protein is embedded.Results
In order to offer an alternative to the classical amyloid-like IBs, here we develop functional IBs exploiting the coiled-
SUBMITTER: Gil-Garcia M
PROVIDER: S-EPMC7268670 | biostudies-literature | 2020 Jun
REPOSITORIES: biostudies-literature