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DNA Findings Hold Potential for Cancer Treatment

Oct. 8, 2012 — Six years ago, Boise State University biology professor Greg Hampikian and computer science colleague Tim Andersen announced that they had identified tiny DNA and protein sequences that were absent in nature. Hampikian termed these sequences ‘nullomers’ and a headline in the New Scientist magazine proclaimed the sequences as “DNA Too Dangerous to Exist.”


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The researchers proposed that these sequences could have properties that were incompatible with life, and might serve as drugs to kill pathogens and even cancer. New research findings suggest this may be true.

The October issue of the online journal Peptides will publish the first results of nullomer-based drugs. They show that these compounds kill breast and prostate cancer cells in the laboratory. More significantly, while their lethal effects on cancer cells increase over time, nullomer effects on normal cells decrease over time.

“We have a long way to go, but we finally have proof that nullomers have biological effects that can benefit human health,” Hampikian said.

Hampikian is known internationally for his work in DNA forensics, and he played a key role in the exoneration of Amanda Knox, the American college student convicted of the 2007 murder of her roommate in Perugia, Italy. In his Boise State lab, Hampikian and student and faculty collaborators work on diverse DNA projects, including developing new cancer drugs, discovering new species of single-celled organisms in Idaho, studying Basque sex chromosomes and inventing micro devices.

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The above story is reprinted from materials provided by Boise State University, via Newswise.

Note: Materials may be edited for content and length. For further information, please contact the source cited above.


Journal Reference:

  1. Abdelkrim Alileche, Jayita Goswami, William Bourland, Mike Davis, Greg Hampikian. Nullomer derived anticancer peptides (NulloPs): Differential lethal effects on normal and cancer cells in vitro. Peptides, 2012; DOI: 10.1016/j.peptides.2012.09.015
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