Nine current and former Hamilton chemistry students published an article in the International Journal of Quantum Chemistry with former postdoctoral associate Steve Feldgus, co-director of the Center for Molecular Design Karl Kirschner, and Winslow Professor of Chemistry George Shields. The students involved were Katrina Lexa '05, Katherine Alser '09, Amanda Salisburg '08, Damien Ellens '03, Lorena Hernandez '03, Sam Bono '00, Heather Michael '07, Jennifer Derby '01, and Jaime Skiba '02. Their research article, "The Search for Low Energy Conformational Families of Small Peptides: Searching for Active Conformations of Small Peptides in the Absence of a Known Receptor," is the result of six years of research.
The project was started by Bono and Hernandez in the summer of 2000, thanks to a beginning collaboration with former Professor of Biology Steve Festin. Bono, Derby, Skiba, and Ellens devoted their senior thesis work to trying to solve the problem of how these peptides were able to inhibit breast cancer. Feldgus, a postdoctoral associate supported by the Dreyfus Foundation from 2000 to 2002, worked with Derby, Skiba, Hernandez, and Lexa on the project while he was here. In the summer of 2004 Michael and Lexa showed that the Monte Carlo method with the OPLS force field would not work. Lexa continued work on the project for her senior thesis, and near the end of the 2004-05 academic year, working closely with Kirschner, they implemented a new methodology known as Replica Exchange Molecular Dynamics which gave the first glimmer of success. Salisburg and Alser helped finish the complicated analysis in the summers of 2005 and 2006.
The paper, primarily written by Lexa and Kirschner, outlines the methodology used during the course of this investigation, and reveals that all active peptides that inhibit breast cancer have a unique turn structure. The researchers hypothesize that this structure interacts with an unknown receptor that is activated during estrogen-dependent breast cancer. The paper can be viewed here: http://www3.interscience.wiley.com/cgi-bin/abstract/114292413/ABSTRACT
This research was supported by the National Science Foundation, the National Cancer Institute (part of NIH), the Department of Defense's Breast Cancer Research Program, Research Corporation, ACS/PRF, the New York State Breast Cancer Research and Education Fund, and Hamilton College.
The project was started by Bono and Hernandez in the summer of 2000, thanks to a beginning collaboration with former Professor of Biology Steve Festin. Bono, Derby, Skiba, and Ellens devoted their senior thesis work to trying to solve the problem of how these peptides were able to inhibit breast cancer. Feldgus, a postdoctoral associate supported by the Dreyfus Foundation from 2000 to 2002, worked with Derby, Skiba, Hernandez, and Lexa on the project while he was here. In the summer of 2004 Michael and Lexa showed that the Monte Carlo method with the OPLS force field would not work. Lexa continued work on the project for her senior thesis, and near the end of the 2004-05 academic year, working closely with Kirschner, they implemented a new methodology known as Replica Exchange Molecular Dynamics which gave the first glimmer of success. Salisburg and Alser helped finish the complicated analysis in the summers of 2005 and 2006.
The paper, primarily written by Lexa and Kirschner, outlines the methodology used during the course of this investigation, and reveals that all active peptides that inhibit breast cancer have a unique turn structure. The researchers hypothesize that this structure interacts with an unknown receptor that is activated during estrogen-dependent breast cancer. The paper can be viewed here: http://www3.interscience.wiley.com/cgi-bin/abstract/114292413/ABSTRACT
This research was supported by the National Science Foundation, the National Cancer Institute (part of NIH), the Department of Defense's Breast Cancer Research Program, Research Corporation, ACS/PRF, the New York State Breast Cancer Research and Education Fund, and Hamilton College.
