Directed evolution and biophysical characterization of a full-length, soluble, human caveolin-1 variant.

ABSTRACT: Protein engineering by directed evolution can alter proteins' structures, properties, and functions. However, membrane proteins, despite their importance to living organisms, remain relatively unexplored as targets for protein engineering and directed evolution. This gap in capabilities likely results from the tendency of membrane proteins to aggregate and fail to overexpress in bacteria cells. For example, the membrane protein caveolin-1 has been implicated in many cell signaling pathways and diseases, yet the full-length protein is too aggregation-prone for detailed mutagenesis, directed evolution, and biophysical characterization. Using a phage-displayed library of full-length caveolin-1 variants, directed evolution with alternating subtractive and functional selections isolated a full-

SUBMITTER: Smith JN 

PROVIDER: S-EPMC6269214 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature