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Small molecule receptor detects lipid's telltale sign of cell death
Date:9/12/2011

atients," Gao said.

The cLac molecule is relatively small, built upon on a cyclic peptide scaffold of approximately a dozen amino acids, yet Gao's laboratory tests show it is capable of capturing the lipid molecule phosphatidylserine (PS) a function nature accomplishes by using proteins of several hundred amino acids, Gao said. In apoptotic cells PS flows to the surface where cLac is able to latch onto the dying cells while bypassing living cells. In the current report, researchers colored cLac with a fluorescent dye in order to highlight apoptotic cells for fluorescence microscopy. By using appropriate tracing agents, cLac should be detectable through commonly used imaging technology, including MRI and PET.

The cLac molecule could offer a cost-effective, more stable and cleaner alternative to natural PS-binding proteins used for similar purposes, Gao said. Those proteins are bulky and relatively unstable, contain metal cofactors that make results difficult to interpret and show poor ability to penetrate tissue because of their size.

Gao said cLac could also serve as a useful tool for researchers who use protein as a cell death indicator to screen for millions of compounds. The use of the small, peptide-binding molecule could substantially reduce costs for researchers, Gao said.


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Contact: Ed Hayward
ed.hayward@bc.edu
617-552-4826
Boston College
Source:Eurekalert  

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