The cobalt-albumin binding assay: insights into its mode of action.

Background: We previously hypothesized that the N-terminus of human serum albumin (HSA) is altered during ischemic events, thus establishing the foundation for the cobalt-HSA binding assay phenomenon. In this investigation, we attempt to clarify the mode of action of the cobalt-HSA binding assay by direct observations of cobalt binding to HSA.

Methods: High pressure liquid chromatography coupled to positive electrospray ionization mass spectrometry (HPLC/MS) was used to study cobalt binding to HSA in the plasma of patients with and without evidence of myocardial ischemia.

Combined cupric- and cuprous-binding peptides are effective in preventing IL-8 release from endothelial cells and redox reactions.

Copper mobilization and subsequent redox reactions have been implicated in the pathogenesis of numerous inflammation-based diseases. Reduction of the cupric ion (Cu(2+)) to the cuprous ion (Cu(+)) is necessary for the production of copper-induced reactive oxygen species (ROS). Peptides, designed to bind both Cu(2+) and Cu(+) and have the ability to prevent copper redox reactions, were studied.