Basic and translational research on cancer, and development of new cancer therapeutics, has focused on different aspects of cancer cellular function. One area of focus is the life and death of a cancer cell. Apoptosis, also known as programmed cell death, is a fundamental process of cells including cancer cells. The signal transduction pathways of apoptosis involve many different proteins and their interactions with each other. Protein-protein interactions involved in these apoptotic signals, like those in many other biological processes, are often determined or influenced by a short fragment of protein sequence or even certain key amino acid residues with important functional or structural roles in the protein-protein interface. For biomedical and pharmaceutical scientists, developing new molecular tools to understand and control the functions of these small protein fragments or residues and the biological and pathological processes that they mediate is a task and challenge of both fundamental interest and practical value.
In the work published in the February issue of Experimental Biology and Medicine, Huang, Zhang, Reed, An and their coworkers have developed new synthetic molecules as models to study the structural and functional role of the proline residue and tetrapeptide sequence important for the regulation of cancer cell apoptosis by the XIAP protein. The work was carried out jointly by the laboratories of Ziwei Huang and Jing An, formerly at the Sanford-Burnham Medical Research Institute in La Jolla, California and now the Cancer Research Institute and Department of Pharmacology of the State University of New York (SUNY) Upstate Medical University in Syracuse, New York, Liangren Zhang at Peking University School of Pharmaceutical Sciences in Beijing, China, and John Reed at Sanford-Burnham Medical Research Institute.
Dr. Huang, who led this international research team, stated "research on protein-protein interactions a
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Society for Experimental Biology and Medicine