Researchers have constructed a protein out of amino acids not found in natural proteins, discovering that they can form a complex, stable structure closely resembling 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 the 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.
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 -amino acid monomers that were used to prepare the synthetic protein.
Schepartz and colleagues built the short protein, or peptide, from -amino acids, which, although they exist in cells, are never found in ribosomally produced proteins. -amino acids differ from the -amino acids that compose natural proteins by the addition of a single chemical componenta methylene groupinto the peptide backbone.
"The fundamental insight from this study is that -peptides can assemble into structures that generally resemble natural proteins in shape and stability," Schepartz said. She added that their findings about the structure of the molecule that she and her colleagues synthesized will help scientists construct more elaborate -peptide assemblies and ones that possess true biologic function.
Such -peptides could also be designed as pharmaceuticals that would be more effective than natural protein drugs, because the enzymes that degrade natural p
'"/>
Contact: Jennifer Donovan
donovanj@hhmi.org
301-215-8859
Howard Hughes Medical Institute
6-Feb-2007