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February 5, 2007
Volume 85, Number 6
p. 7

Foldamers

Synthetic Protein Mimics Real Thing

β-Amino acid-based assembly has hallmarks of a true protein

Stu Borman

IN THE CLASSIC TALE "Pinocchio," the wood-carver Gepetto made a puppet that turned out to act just like a real boy. In the same spirit of creativity, researchers have created the first nonprotein oligomer that has been verified experimentally to look and act much like a true protein (J. Am. Chem. Soc. 2007, 129, 1532).

Reprinted from JACS (both)
Ribbon diagram (top) of β-peptide bundle shows its overall architecture, and partially space-filling representation (bottom) shows how its β-homoleucine residues (green) form a well-packed hydrophobic core.

Nonproteins that act like proteins have long been sought for their potential use for a range of biomedical applications, including the design of proteinlike therapeutics that wouldn't be degraded by enzymes and could therefore be administered orally.

Chemistry professor Alanna Schepartz and coworkers Douglas S. Daniels, E. James Petersson, and Jade X. Qiu at Yale University have now created such a proteinlike structure, a β-peptide bundle. And they show that it exhibits several hallmarks of real proteins, including exceptional stability, an interior core of water-shunning amino acid side chains, and the