Troy, N.Y. It has been an exciting time for Rensselaer Polytechnic Institute student Kinsley French. During the Rensselaer commencement, French was awarded the J. Erik Jonsson Prize for her perfect 4.0 grade point average and high-caliber undergraduate research. She earned a dual major in mathematics and biology in just three and a half years.
Just weeks before, French received the exciting news that she had earned a graduate research award from the National Science Foundation (NSF) to pursue her research into proteins and HIV transmission while she works toward her doctoral degree at Rensselaer. The award, which goes to only a select few graduate students around the nation, will help cover French's tuition, fund her research, and provide her a stipend while she pursues her Ph.D.
"I would, without hesitation, put Kinsley as the best overall of all students that I worked with during 20 years of my academic career at some of the best schools in the United States," said French's adviser George Makhatadze, Constellation Professor in Biocomputation and Bioinformatics "It seems to me that Kinsley excels in everything she does. She maintained a 4.0 GPA and is first in her class at RPI, while pursuing dual major. She is fantastic in the lab, and she even finds time to do significant amounts of outreach in the rural parts of upstate New York as a math and science tutor."
Kinsley has been working in Makhatdze's lab since her junior year. Her research focuses on how proteins in the body sometimes clump together, a process called aggregation. This seemingly simple biochemical process actually involves many different mechanical and chemical interactions in the body and is responsible for many of the degenerative illnesses that humans currently face, from Alzheimer's disease to diabetes. Kinsley is currently studying how a specific type of protein aggregate called amyloid fibrils might play a role in the transmission of HIV by men.
A specific type of protein fragment called PAPf39 is formed from a protein secreted by the male prostate. That fragment has been found to form fibrils that increase the transmission of HIV by up to 100,000 times over its non-aggregated form. French is currently studying how and under what conditions the less virulent single fragments or monomers of PAPf39 come together or aggregate to create what appears to be a much more potent vehicle for transmitting the deadly virus.
"By understanding how the aggregates are formed, we can lay the foundation to better understand how HIV is transmitted," French said. "And by understanding that process, we hope to begin putting the pieces in place to hopefully develop a new therapeutic against HIV transmission."
Her research has already been published in the journal Biochemistry and will continue with the new NSF funding. The research under the NSF program will be a broad study of how proteins form aggregates with implications for medicine as well as industries that rely on proteins in their products.
French grew up in Cherry Plain, N.Y., as one of six children. She is an active mentor and tutor in her community as well as a certified lifeguard.
|Contact: Gabrielle DeMarco|
Rensselaer Polytechnic Institute