Metal ions biological surface, interaction with

Protein-protein interactions usually occur on the surface of proteins where mainly loops or turns are present [24], It is, therefore, of interest to stabilize specific peptide turns and test them for their biological activity [25-28], As discussed, metal coordination seems to be a powerful tool for obtaining macrocycles with a bent peptidic domain simply by mixing metal ions and peptide-bridged ligands. 

Chemical investigations of this biological system have attempted to address the following questions (1) What is the microstructure of the hydrated Si02 within costal rods (2) How are the costal rods linked together in the intact basket (3) What is the nature of the surface silica in the costal rods These questions were answered in some part by studies of intact and partially intact loricae, on demineralized costae, and by considering the nature of the interaction between metal ions (Fe, Co +), colloidal silica, and liposomes with the costal strips. 

There has been considerable interest in recent years in the formation of condensed films of purine and pyrimidine bases at the solid-liquid interface. It is well recognised that non-covalent affinities between base pairs play a prevalent role in determining nucleic acid conformation and functionality. Likewise, there has been interest in the role of substrate and non-covalent intermolecular interactions in the configuration of ordered monolayers of purine and pyrimidine bases. There is also more general interest in the interaction of bases with metal surfaces and metal complexes. In the latter case it is noted that the biological role of nucleic acids and certain nucleotides are dependent on metal ions, particularly Mg, Ca, Zn, Mn, Cu and Ni. " Also certain metal complexes, notably of platinum, have the anti-tumour activity, which is linked to their ability to bind to bases on DNA. On a different note, the possibility that purine-pyrimidine arrays assembled on naturally occurring mineral surfaces might act as possible templates for biomolecular assembly has been discussed by Sowerby et al. 

Some typical biological interactions, frequently used in affinity chromatography are enzyme to substrate analogue, inhibitor, or cofactor antibody to antigen, virus, or cell lectin to polysaccharide, glycoprotein, cell surface receptor, or cell nucleic acid to complementary base sequence, histones, or nucleic acid polymerase hormone or vitamin to receptor, or carrier protein glutathione to glutathione-S-transferase (GST) or GST fusion proteins and metal ions to poly (His) fusion proteins, or native proteins with histidine, cysteine and/or tryptophan residues on their surfaces. 

Molecular-level studies of chemistry in solution and at interfaces, including mineral interfaces (e.g., the behavior of metal ions in aqueous solution and on metal oxide or clay surfaces for vadose zone, tank, and groundwater remediation and catalysis)—a detailed understanding of redox (electron transfer chemistry) is broadly needed studies of the interactions of biological molecules with surfaces for bioremediation are also needed and being pursued. 

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