Specific GFP-binding artificial proteins (αRep): a new tool for in vitro to live cell applications.

ABSTRACT: A family of artificial proteins, named αRep, based on a natural family of helical repeat was previously designed. αRep members are efficiently expressed, folded and extremely stable proteins. A large αRep library was constructed creating proteins with a randomized interaction surface. In the present study, we show that the αRep library is an efficient source of tailor-made specific proteins with direct applications in biochemistry and cell biology. From this library, we selected by phage display αRep binders with nanomolar dissociation constants against the GFP. The structures of two independent αRep binders in complex with the GFP target were solved by X-ray crystallography revealing two totally different binding modes. The affinity of the selected αReps for GFP proved sufficient for prac

SUBMITTER: Chevrel A 

PROVIDER: S-EPMC4613692 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature