The biological relevance of proteins and peptides for Cu(II) biology, including the extracellular transport of this element, is commonly estimated by studying stabilities and structures of their complexes. However, our experimental studies on the kinetics of formation of Cu(II) complexes of ATCUN/NTS and Xaa-His-R peptides, considered to be key actors in extracellular copper biology, revealed novel long-lived reaction intermediates. These intermediates, rather than the final reaction products fulfil the chemical criteria for actual biocomplexes derived from biological studies. Our research clearly demonstrated that understanding of the kinetic aspect of interactions is indispensable for realistic modeling of biological interactions of metal ions.
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Sample pre-treatment is a very important step in many analytical procedures, especially when the analyte is presented in low concentration in complex sample matrices. In this paper, potential using of the supported liquid membrane (SLM) technique as a sample preparation step in order to isolate, pre-concentrate and separate small peptides and phosphono dipeptides from aqueous solutions and body fluids is discussed. An influence of various parameters including carrier type, donor and acceptor phase compositions, presence of salts and proteins in analysed samples on extraction efficiency and selectivity is presented. Additionally, comparison of SLM extraction efficiency from aqueous samples and body fluids is presented. Finally, a fully automated system consisted of SLM extraction coupled on-line with HPLC-UV for the analysis of selected peptides from blood plasma is shown.
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