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Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity
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Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity
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Journal Article
Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity
2014
Overview
Mirror-image proteins (composed of d -amino acids) are promising therapeutic agents and drug discovery tools, but as synthesis of larger d -proteins becomes feasible, a major anticipated challenge is the folding of these proteins into their active conformations. In vivo, many large and/or complex proteins require chaperones like GroEL/ES to prevent misfolding and produce functional protein. The ability of chaperones to fold d -proteins is unknown. Here we examine the ability of GroEL/ES to fold a synthetic d -protein. We report the total chemical synthesis of a 312-residue GroEL/ES-dependent protein, DapA, in both l - and d -chiralities, the longest fully synthetic proteins yet reported. Impressively, GroEL/ES folds both l - and d -DapA. This work extends the limits of chemical protein synthesis, reveals ambidextrous GroEL/ES folding activity, and provides a valuable tool to fold d -proteins for drug development and mirror-image synthetic biology applications.
Publisher
National Academy of Sciences
