Newswise — During her time at Rensselaer as a doctoral student in biochemistry and biophysics, Melissa Kemp has worked on research that has drawn international attention and could help protect the lives of millions of people. With 10 publications and a submitted patent, the young scientist has already helped develop research that has implications for drug safety, spinal injury repair, and malaria prevention.
Following the death of more than 80 people around the world from contaminated batches of the blood thinner heparin, Kemp went to work in the lab of Robert Linhardt, one of the foremost experts on heparin and the Ann and John H. Broadbent Jr. '59 Senior Constellation Professor of Biocatalysis and Metabolic Engineering at Rensselaer. Linhardt was among the scientists to discover the contamination known as oversulfated chondroitin sulfate, which has a structure so similar to heparin it was nearly undetectable. Kemp was involved in studying the detection of contaminant using five methods commonly utilized by drug manufacturers. Kemp and collaborators found that two of these methods would fail to accurately detect the sneaky contaminant. She said she hopes that companies using these methods take extra precautions in detecting the presence of contaminant. Kemp also worked with Linhardt to study heparin-protein interactions using a technique called surface plasmon resonance (SPR). She worked on the formulation of a synthetic heparin by screening its interaction with other proteins, which was one of the first steps in making a purely synthetic heparin. Conventional heparin is derived from animal tissues, while synthetic heparin is considered a safer alternative as it's made completely in a controlled laboratory setting.
"These experiments provided proof of concept that heparin could in fact be created chemoenzymatically, meaning that we could develop a batch of heparin in the lab without using animal sources," she said.
In addition to her work on heparin, Kemp remains heavily involved in research to stop the spread of malaria at its source. The findings could help stop any man, woman, or child from needing to take a drug. Kemp again worked alongside Linhardt and colleagues to isolate a complex carbohydrate called heparan sulfate in mosquitoes, which Linhardt had previously discovered to be the transporter of the disease in the human body. The team wanted to see if heparan sulfate was also present in the mosquito and displayed the same behavior of interaction as the heparan sulfate in humans.
Kemp helped lead the effort to determine the binding activity of the carbohydrate in the organism and how it developed and migrated in the mosquito. She discovered that heparan sulfate was also present in the disease-spreading organs of the mosquito, including the salivary glands, and has the ability to interact with the critical protein on the parasite. She is currently working to determine other molecules that are directly involved in the heparan sulfate-protein interactions in the organism in the hopes of developing a method or drug that could stop its progress and prevent the spread of the disease directly in the mosquito.
Kemp is also working with nanotechnologies to help heal spinal cord injury. In particular, she is using nano-supports to immobilize and stabilize a protein known as chondroitinase. Chondroitinase has been previously discovered to improve spinal cord injury in animal models, but thus far it has been difficult to use even experimentally because it is highly unstable after only a short period of time. Kemp and her collaborators hope that the nano-support will keep the material more stable and improve its localization in the body.
Kemp grew up in Milton, N.Y., across the river from Poughkeepsie with her older brother. She received a bachelor's in computer science from Pace University. She is a member of several high-level scientific societies and is currently looking for a post-doctoral position in molecular biology to supplement her experience in chemistry. She said she hopes to build a career working in the laboratory environment.
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