Aluminium speciation in relation to aluminium bioavailability, metabolism and toxicity

Publisher Summary This chapter discusses copper complexes that offer a physiological approach to the treatment of chronic diseases. Copper is recognized as an essential metalloelement just as sodium, potassium, magnesium, calcium, iron, zinc, chromium, vanadium, and manganese. Just as essential amino acids, essential fatty acids and essential cofactors (vitamins), essential metalloelements are required for normal metabolic processes but cannot be synthesized de novo, and daily dietary intake and absorption are required. The adult body contains between 1.4 mg (22 pmol) and 2.1 mg (33 pmol) of copper per kilogram of body weight while the infant body contains three times this amount, consistent with the fact that infant metabolic needs are that much greater than those of adults. The essentiality of copper is now understood as being based upon its recognized need for activation of copper-dependent enzymes. Complexed forms of copper also facilitate absorption, tissue distribution, and tissue utilization. In the nondisease state, these forms of copper account for the physiologic regulation of copper-dependent homeostatic processes. Consistent with the newly found role for copper in synthesis of neuroendocrine peptides, the copper complex of histidine has been found to increase the secretion of luteinizing hormone-releasing hormone (LH-RH) from granules of the median eminence.

Copper complexes offer a physiological approach to treatment of chronic diseases.

Intrinsic stoichiometric equilibrium constants for the binding of zinc(II) and copper(II) to the high affinity site of serum albumin.

Amyloid-β: an antioxidant that becomes a pro-oxidant and critically contributes to Alzheimer’s disease

Chemical speciation studies in relation to aluminium metabolism and toxicity

Although the absolute concentrations of metal complexes in blood plasma are controlled by protein binding, the percentage distribution of transition metal ions amongst low molecular weight ligands is not. Thus, computer simulations which omit protein equilibria can nevertheless afford reliable information about such metals in the biofluid.

P. M. May

Papers

Ambivalent effect of protein binding on computed distributions of metal ions complexed by ligands in blood plasma.