( Structure of the Zwit-1F beta-peptide b...)Man-Made Proteins Could Be More Useful Than Real Ones,Health

Structure of the Zwit-1F beta-peptide bundle as determined by x-ray crystallography. The bundle contains eight copies of the beta-peptide Zwit-1F with parallel //and antiparallel helices in like and unlike colors, respectively.

Researchers have constructed a protein out of amino acids not found in natural proteins, discovering that they can form a complex, stable structure that closely resembles a natural protein. Their findings could help scientists design drugs that look and act like real proteins but won't be degraded by enzymes or targeted by th e immune system, as natural proteins are.

The researchers, led by Howard Hughes Medical Institute (HHMI) professor Alanna Schepartz, report their findings in the February 14, 2007, issue of the Journal of the American Chemical Society, published in advance online on January 19, 2007. Schepartz and her coauthors, Douglas Daniels, James Petersson, and Jade Qiu, are all at Yale University. A story in the February 5, 2007, issue of Chemical & Engineering News spotlighted the research.

“The fundamental insight from this study is that beta-peptides can assemble into structures that generally resemble natural proteins in shape and stability.” Alanna Schepartz.

As an HHMI professor, Schepartz received a $1 million grant to find ways to infuse undergraduate teaching with the excitement of research. Several of her HHMI undergraduates synthesized beta-amino acid monomers that were used to prepare the synthetic protein.

Schepartz and colleagues built the short protein, or peptide, from a-amino acids, which, although they exist in cells, are never found in ribosomally produced proteins. a-amino acids differ from the alpha-amino acids that compose natural proteins by the addition of a single chemical component—a methylene group—into the peptide backbone.

“The fundamental insight from this study is that a-peptides can assemble into structures that generally resemble natu
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