MOLECULAR SLEUTH: Mary Ann McLane, an assistant professor within the University of Delaware's Department of Medical Technology, is investigating the structure of the disintegrin, eristostatin, to learn exactly how it prevents the spread of tumors in laboratory mice. Her investigations, though preliminary, may help pharmaceutical companies develop new cancer-fighting drugs.
Photo by Jack Buxbaum
SALVE FROM SERPENTS? Venom from viper-type snakes, such as the white-lipped viper in these photographs, contain disintegrins--proteins that interact with a family of cellular receptors called integrins. Disintegrins inhibit an early step in blood clotting by preventing the sticky protein, fibrinogen, from binding with integrins on platelets. And, the disintegrin eristostatin, from Macmahon's Viper (Eristocophis macmahoni), keeps tumors from spreading in mice, says Mary Ann McLane, an assistant professor within the University of Delaware's Department of Medical Technology.
Snake Photos by John H. Tashjian of San Marcos, Ca.
DOUBLE TROUBLE: Two viper-venom disintegrins, echistatin (left) and eristostatin (right), are 68 percent identical, reports Mary Ann McLane, an assistant professor within the Department of Medical Technology at the University of Delaware. Yet, only eristostatin prevents the spread of tumors in mice. McLane is comparing structural differences between the two proteins, to learn why eristostatin is "selective," while echistatin is "promiscuous," binding with many receptors.
Protein Structures Courtesy of Senadi Vijay-Kumar