Chemical Reviews, 1999, Vol. 99, No. 9 7A
In Color on the Front Cover (Top) One side of a German DM200 bill, showing Paul Ehrlich, the father of immunology and of the structure−activity ratio, and the structure of hexa(phenylarsenic), a model compound for Ehrlich 606. See “Vanadium Compounds as Insulin Mimics” by Katherine H. Thompson, John H. McNeill, and Chris Orvig, p 2561. (Bottom) Structure of AngioMARKsa prototypic targeted contrast agent for magnetic resonance imaging (MRI) currently undergoing clinical trials. The hydrophobic bicyclohexyl moiety targets the plasma protein serum albumin, the octadentate moiety sequesters the toxic metal ion, and the paramagnetic gadolinium(III) ion and exchangeable water molecule provide relaxation enhancement for contrast MRI. See “Gadolinium(III) Chelates as MRI Contrast Agents: Structure, Dynamics, and Applications” by Peter Caravan, Jeffrey J. Ellison, Thomas J. McMurry, and Randall B. Lauffer, p 2293. In Color on the Inside Back Cover (Top) Two strategies of Radiopharmaceutical Design. See “99mTc-Labeled Small Peptides as Diagnostic Radiopharmaceuticals” by Shuang Liu and D. Scott Edwards, p 2235. (Center) Cellular processing of cisplatin−DNA adducts. See “Structure, Recognition, and Processing of Cisplatin−DNA Adducts” by Elizabeth R. Jamieson and Stephen J. Lippard, p 2467. (Bottom left) The blood protein transferrin mediates the delivery of therapeutic and diagnostic metal ions to cells and is shown here with iron bound to the C-lobe and a vacant (cleft-open) N-lobe site; the strength of the metal binding correlates with metal ion activity. See “Transferrin as a Metal Ion Mediator” by Hongzhe Sun, Hongyan Li, and Peter J Sadler, p 2817. (Bottom right) Extensive and widespread use of bismuth compounds in medicine is currently highlighted by the use of colloidal bismuth subcitrate and bismuth subsalicylate in the treatment of gastrointestinal disorders. See “Bismuth Compounds and Preparations with Biological or Medicinal Relevance” by Glen G. Briand and Neil Burford, p 2601. In Color on the Back Cover (Top left) Cobalt complex occupies the active site of thermolysin. See “Metal Complexes as Enzyme Inhibitors” by Angelique Y. Louie and Thomas J. Meade, p 2711. (Top center) Structure of the bioactive Schiff-base phenolate iron(III) complex predicted on the basis of molecular modeling. See “Metal Complexes for Therapy and Diagnosis of Drug Resistance” by Vijay Sharma and David Piwnica-Worms, p 2545. (Top right) View of an NMR sequence of ∆-R-[Rh[(R,R)Me2trien]phi]3+ bound 5′-GAGTGCACTC-3′. See “Recognition and Reaction of Metallointercalators with DNA” by Kathryn E. Erkkila, Duncan T. Odom, and Jacqueline K. Barton, p 2777. (Bottom left) Metal complexes such as the amphiphilic, trisulfophthalocyanine strongly absorb red light resulting in the formation of a long-lived triplet state. Interaction with molecular oxygen produces cytotoxic species, including singlet oxygen, which are responsible for the photodynamic effect. See “Metal Complexes as Photo- and Radiosensitizers” by Hasrat Ali and Johan E. van Lier, p 2379. (Bottom center) Glutathione complex of Ru(III)senergy-minimized structure for the peptide portion of [(GS)(NH3)5RuIII]+. The metal ion was constrained to be octahedral with Ru−NH3 bond distances of 2.11 Å. No solvent molecules were included. See “Non-Platinum Chemotherapeutic Metallopharmaceuticals” by Michael J. Clarke, Fuchun Zhu, and Dominic R. Frasca, p 2511. (Bottom right) Representation of marimastat (12) bound human MMP-1. See “Design and Therapeutic Application of Matrix Metalloproteinase Inhibitors” by Mark Whittaker, Christopher D. Floyd, Peter Brown, and Andrew J. H. Gearing, p 2735.
