Bobby Abdallah wins second place at 2011 MGE@MSA Student Research Conference…
The Spring 2011 More Graduate Education at Mountain States Alliance (MGE@MSA) Student Research Conference was held at ASU earlier this year. Recently Bobby Abdallah, an incoming graduate student supervised by Alexandra Ros, received notification that he had won second prize for his poster on hydrophobic valves in microfluidic devices. He was selected from a group of more than 100 undergraduates from around the U.S. who attended the meeting.
The MGE@MSA Student Research Conference was created to encourage underrepresented undergraduates to pursue graduate studies in their respective fields through a series of seminars and a competitive poster session. Those eligible for this conference are undergraduate and graduate students in good standing who create a poster based on their current research. The second place prize included a monetary award as well as a certificate and recognition within the program.
Awardees are chosen on the basis of the quality and significance of their research, as well as the quality of their presentation. Bobby presented his poster on the research project he undertook in Ros’s lab as an undergraduate. He developed and refined a method to introduce a hydrophobic valve in microfluidic channels to prevent capillary action. "His work is an important step towards producing reproducible microchip systems for nano-crystallization studies of membrane proteins, a project funded by the National Institute of Health," explained Alexandra Ros.
| Anindya Roy and Sandip Shinde were recently awarded a travel grant by the American Peptide Society to attend the American Peptide Symposium in San Diego, Ca, June 24-30. The awards covered registration travel expenses, and accommodation.
Anindya presented a poster titled "Denovo Design and Synthesis of Artificial [4Fe-4S] Binding Peptide Motif" Coauthors are Anindya Roy, Iosifina Sarrou, Kevin Redding and Giovanna Ghirlanda.
Abstract: Fe-S] cluster proteins are one of the most abundant and prevalent class of proteins in nature. They carry out a wide variety of biological functions such as redox catalysis, non-redox catalysis, gene expression and oxygen sensing. In this particular project, we are utilizing de novo designed peptides to develop artificial supramolecular peptide framework with multiple redox cofactor binding sites. DSD,a domain swapped homodimeric denovo designed 3 helix bundle peptide was our first generation peptide for [4Fe-4S] cluster incorporation. By rational design on the peptide scaffold, two [4Fe-4S] cluster binding sites were introduced at two ends of the bundle.
Sandip presented a poster titled: "Modulation of function in Heme binding membrane protein", Coauthors are Sandip Shinde, Jeanine Cordova, Christopher Halsey, Jason Cooley and Giovanna Ghirlanda.
|Abstract: De novo designed heme binding proteins have been used successfully to recapitulate features of natural hemoproteins. This approach is now been extended to membrane soluble model proteins. Our group designed a functional hemoprotein, ME1, by engineering a bis-histidine binding site into a natural membrane protein, Glycophorin A (Cordova et al., JACS 2007). Here, we investigate the effect of hydrophobic and aromatic residues in modulating the redox potential in the context of a membrane-soluble model system. ME1 binds Fe(III) Protoporphyrin IX with submicromolar affinity, has a redox potential of –128 mV, and displays nascent peroxidase activity. We designed aromatic interactions to the heme through a single-point mutant, G25F, in which a phenylanine is designed to dock against the porphyrin ring. This mutation lowers the redox potential of the cofactor to -172 mV, and results in roughly 10 fold tighter binding to Fe(III)-Protoporphyrin IX (Kd,app of 6.5 x 10-8 M). We ascribe these effects to a direct stabilization of the Fe(III) form, which supersedes changes in the hydrophobic environment of the heme. Our work demonstrates that specific design features aimed at controlling the properties of bound cofactors can be introduced in a minimalist membrane hemoprotein model. The ability to modulate the redox potential of cofactors embedded in artificial membrane proteins is crucial for the design of electron transfer chains across membranes in functional photosynthetic devices.
Biochemistry major makes strides in fight against cancer
ake a tour of ASU's Virginia G. Piper Center for Personalized Diagnostics and you'll find some of the most advanced technology available in the scientific world. But you won't just find tenured professors with stacks of published papers conducting research here. You'll also see ambitious undergraduates like Paul Akhenblit, a biochemistry major helping to make strides in cancer research.
Akhenblit works in the LaBaer Lab, directed by Joshua LaBaer, a leader in the field of personalized medicine. Before coming to ASU, LaBaer directed the Harvard Institute of Proteomics lab. There, he and his colleagues developed a way to study the human proteome, or all of the proteins in a person's body.
Proteins are found in human DNA and can provide clues about a person's health. The technology that LaBaer developed, called Nucleic Acid-Programmable Protein Array (NAPPA), may lead to earlier detection of several diseases, including cancer.
"In the context of many diseases, patients sometimes produce antibodies against specific proteins related to the disease," LaBaer says.
If you've ever had chicken pox, your body has produced antibodies to attack it. Those antibodies are still detectable in your blood, even years later. Similarly, someone with cancer or diabetes produces antibodies against specific proteins related to those diseases. The antibodies show up in the person's blood before the disease does, so identifying them could lead to earlier detection of the disease.
To study this reaction, Akhenblit and other researchers create a protein microarray, or a "protein chip," which is a glass microscope slide imprinted with thousands of different DNA sequences. These translate into thousands of different protein molecules. The DNA comes from both healthy people and people with some type of disease, such as breast cancer.
"In the traditional way of creating a protein microarray, we had to isolate the protein of interest and purify, amplify and store it," Akhenblit says. That method was expensive and time-consuming, even with a simple protein. Using NAPPA, researchers are able to study many proteins all at the same time. Five glass slides can hold 10,000 of a person's proteins. This is called the "10k collection."
Researchers add a serum to the slides and look for a reaction from the proteins. The serum is blood with no red or white blood cells, taken from mice that were afflicted with some type of cancer. The mouse blood contains antibodies that were produced to fend off that cancer. By observing the reaction caused by the serum, the scientists are hoping to identify biomarkers.
"A biomarker is some kind of molecule that gives away its presence during a certain condition," Akhenblit says. If antibodies in the serum react with certain proteins in the DNA of people with cancer, but do not react with those proteins in people without cancer, the identified proteins can serve as biomarkers.
So far, researchers at the LaBaer lab have identified 28 biomarkers for breast cancer (see "Scientists aid early detection of breast cancer"). They hope to expand their research to find biomarkers for other types of cancers and diseases, including diabetes and arthritis.
Working in the LaBaer lab was not Akhenblit's first experience as an undergraduate researcher. Starting in his freshman year, he worked at ASU's Magnetic Resonance Research Center, studying spider silk.
"Spider silk is five times stronger than steel. The military has a lot of interest in this for jets – making them super light but also much stronger," Akhenblit says, adding that the silk could also one day be used to replace damaged tendons.
As a biochemistry major planning to pursue a Ph.D. in cancer biology, Akhenblit was pleased with the opportunities for undergraduate research at ASU.
"Coming to ASU is probably the best decision I have made as far as academia goes," he says. "I feel like I was involved with the right research group. It was the right place for me, and I don't think you could go wrong by coming here."
He was also very successful early on in his academic career, says Jeff Yarger, Akhenblit's research advisor during his time at the Magnetic Resonance Center.
"What makes Paul in the top 10 to 20 percent of undergrads I've worked with is his ability and interest in the subject, as far as being self-motivated and curious in learning the material. He wanted to get into the lab and figure things out for himself," Yarger says, adding that for students majoring in lab-based sciences like chemistry and biology, getting involved with research is essential.
"Learning stuff just in the classroom doesn't give students the whole picture of what it's like to have a career in one of those fields," Yarger says.
LaBaer also encourages undergraduate students to participate in research. He explains that while lab courses are designed to give students a certain result on the first try, real research is much more unpredictable. This makes it more difficult, but also more rewarding.
"Real research is really standing at the very edge of human knowledge," LaBaer says. "Everything that you're looking out on in your horizon is stuff that hasn't been done yet, and everything behind you is what's already been done. You're really at that cutting edge."