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DENNIS P. CURRAN Department of Chemistry University of Pittsburgh Pittsburgh, Pa. Like its natural predecessors FK506 and rapamycin, a non-natural immunophilin ligand (506BD) is a potent inhibitor of the FK506 binding protein's rotomase activity. However, unlike the natural compounds, the nonnatural analog does not interfere with T cell activation. Thus, inhibition of rotamase activity is an insufficient requirement for immunosuppressant action. B.E. Bierer, P.K. Somers, T.J. Wandless, S.J. B

Dennis Curran
Jan 6, 1991

DENNIS P. CURRAN

Department of Chemistry
University of Pittsburgh
Pittsburgh, Pa.

Like its natural predecessors FK506 and rapamycin, a non-natural immunophilin ligand (506BD) is a potent inhibitor of the FK506 binding protein's rotomase activity. However, unlike the natural compounds, the nonnatural analog does not interfere with T cell activation. Thus, inhibition of rotamase activity is an insufficient requirement for immunosuppressant action.

B.E. Bierer, P.K. Somers, T.J. Wandless, S.J. Burakoff, S.L. Schreiber, "Probing immunosuppressant action with a non-natural immunophilin ligand," Science, 250, 556-7, 26 October 1990. (Brigham and Women's Hospital, Boston; Dana-Farber Cancer Institute, Boston; Harvard University, Cambridge, Mass.)

Most chemists try to avoid getting their research all tied up in knots. But knots can indeed be beautiful, as illustrated by the X-ray crystal structure of a remarkable synthetic molecule.

C.O. Dietrich-Buchecker, J. Guilham, C. Pascard, J.-P. Sauvage, "Structure of a synthetic trefoil knot coordinated to two copper(I) centers," Angewandte Chemie,...

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