NEWS OF THE WEEK

Cicerone (left), Hobson, Hunt, and Hinojosa.

ACS HONORS LEADERSHIP

PUBLIC SERVICE AWARDS: Society recognizes congressmen and

National Academies' president

THE AMERICAN CHEMICAL Society bestowed its prestigious Public Service Award upon Reps. Ruben Hinojosa (D-Texas), David L. Hobson

(R-Ohio), and National Academies President Ralph J. Cicerone during a Capitol Hill ceremony on April 25.

The awards recognize people who have made out­standing contributions to the development of public

policy that benefits chemistry and the sciences.

"The awards are our way of thanking those who share our pas­sion for science and of recognizing that science and technology are critical to advancing our nation/' said ACS President Catherine (Katie) T. Hunt during opening remarks at the ceremony.

Hinojosa, who chairs the House

Education & Labor Committee's Subcommittee on Higher Education, Lifelong Learning & Competitive­ness, introduced in 2006 the Partnerships for Access to Laboratory Science Act, which the House Science & Technology Committee recently passed. He thanked ACS for its leadership in promoting science, technol­ogy, engineering, and math education.

Hobson, who serves as a ranking member of the Ap­propriations Subcommittee on Energy 8c Water and is a senior member of the Appropriations Subcommittee on Defense, oversaw the first maj or funding increase for ba­sic science at the Department of Energy in a generation.

"By making sound judgments today in research and development, we have an opportunity to transform our national economy and improve the quality of life for future generations," Hobson said.

Cicerone, following a request from the U.S. Senate, led a panel that produced the report "Rising above the Gathering Storm: Energizing and Employing America for a Brighter Economic Future." The report provides a blueprint to increase the nation's ability to innovate.

The awards ceremony was preceded by a poster ses­sion sponsored by the Council on Undergraduate Re­search. Students discussed their research projects with public officials and ACS staff and governance.

The awards were established in 1997 under the leadership of former ACS president Ronald Breslow. —LINDA WANG

DRUG FOR GENETIC DISORDERS

DRUG DEVELOPMENT: Compound might treat conditions caused

oy nonsense mutations

N ONSENSE genetic mutations, which result in shorter-than-normal proteins, cause 5-70% of cases of inherited disorders, including muscular

dystrophy, cystic fibrosis, and cancer. A small molecule now in Phase II clinical trials might be capable of treat­ing several of these types of cases.

This treatment strategy—targeting a group of dis­ease cases caused by one class of mutation rather than

targeting individual diseases—represents a "paradigm shift," according to Stuart W. Peltz, president and CEO of PTC Therapeutics, in South Plainfield, N.J. The biopharmaceuti-cal firm discovered the compound via high-throughput screening.

A nonsense mutation in DNA introduces a code for a stop codon rather than for an amino acid. When the DNA is transcribed into mes­senger RNA (mRNA), this misplaced stop co­don—also known as a premature termination

codon (PTC)—halts translation of the mRNA into a protein by a ribosome. The resulting truncated protein can cause disease. Some cases of Duchenne muscular dystrophy, for instance, are caused by nonsense muta­tions that yield malformed dystrophin, a protein neces­sary for maintaining the strength of muscle fibers.

PTC Therapeutics wants to treat this fatal muscle-wasting disease with the small molecule it calls PTC124. Peltz, University of Pennsylvania physiologist H. Lee Sweeney, and colleagues report that the oral drug binds to ribosomes and allows them to bypass the mRNA site that interrupts dystrophin production. In a mouse model of the disease, the ribosomes then churn out normal, full-length dystrophin, thereby restoring muscle function (Nature, DOI: io.i038/natureo5756). PTC Therapeutics is now testing the compound's ef­ficacy in patients with Duchenne muscular dystrophy and cystic fibrosis.

In a commentary in Nature, Anton Schmitz and Mi­chael Famulok of the University of Bonn, in Germany, point out PTC124/S "astonishing" selectivity for PTCs. The compound enables a ribosome to distinguish between a premature stop codon and a normal stop codon that indicates where protein production should properly cease. The antibiotic gentamycin also allows ribosomes to ignore PTCs, but its severe side effects and intravenous delivery method have limited its use. Furthermore, unlike PTC124, gentamycin increases the risk of producing mutated proteins.—SOPHIE ROVNER

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