The field of bio-inorganic chemistry is at a propitious stage of development. Bio-inorganic chemistry constitutes the interface bertween classical areas of inorganic chemistry and biology. Although biology is generally associated with organic chemistry, inorganic elements are also essential for life processes. Inorganic elements are naturally present in biological systems and act as probes of structure and function. Metal containing compounds are being used not only as biological probes but also as diagnostic and therapeutic
pharmaceuticals. The mechanism of action of platinum anticancer drugs, gold antiarthritic agents and technitium radiopharmaceuticals are some of the topics of investigation in bio-inorganic chemistry.
Prof. Ramesh Chandra has investigated the Tin-protoporphyrin (SnPP) interaction with purified human serum albumin and relationship among the binding of heme, protoporphyrin, bilirubin and SnPP to this protein. He has extended his studies to other metalloporphyrins with BSA, DTT, apomyoglobin, small peptides, peptide hormones, imidazole, RNA and DNA mixed with imidazole and EDTA etc. The studies are useful from a pharmacological point of view since they enhance the selectivity of metal porphyrins for its target and minimize effects on other systems. He has also confirmed that heme binding by serum albumin will be completely unaffected by the presence of SnPP, which does not compromise the ability of serum albumin to bind bilirubin. Both in vitro binding studies and theortical considerations make it highly probable that such an effect could explain the observed amelioration of hyperbilirubinemia (physiological jaundice) with SnPP and SnMP treatment. Recently he has carried out a detailed study on CoMP, CoPP etc. to establish their usefulness in developing the drug for the heme metabolic diseases.
He originated the idea of how metal ions and metalloporphyrins alter the lipid chemistry in organs like liver, kidney, spleen and brain of rats and also the metabolism of phospholipids. He has also studied the in-vivo DNA, RNA and protein synthesis, which are influenced by metalloporphyrins or metal ions. His one of the striking contributions have been for the repairing of hepatic mitochondrial membrane by polyamines, ruptured due to excess of Vitamin A. The main focus of his laboratory is to understand the mode of regulation of heme biosynthesis and catabolism in mammalian cells. Heme, the prosthetic group of all hemoproteins , plays a critical role in the transport of electrons and the oxygen molecule, in the removal of peroxides, in the oxidation of tryptophan, and in the biotransformation of drugs, environmental chemicals and endogenous substrates. There are distinctive aspects in the regulation of genes encoding the erythroid- specific- saminolevulinate synthase (ALAS) and the non-specific ALA synthase (ALA-N), the rate limiting enzymes in heme biosynthesis. We continue our studies on the molecular defects in the human porphyria, i.e. genetic deficiencies of heme pathway enzymes in humans continue in his laboratory.
This laboratory is also involved in the synthesis of various macrocyclic compounds which have similarity with the naturally occurring macrocycles and thereby their metal complexes. The structure of these compounds have been characterized on the basis of various spectral techniques like NMR, IR, UV-visible, Mass and X-ray analysis.
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