Biomedical subjects
Publications and source records attributed to C Bertucci.
C.d. spectra have been measured in aqueous solution to 168 nm for some model compounds related to D-glucopyranose and D-galactopyranose. C.d. difference-spectra reveal the contribution of certain functional groups and confirm contributions for other groups found in earlier work.
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A technique based on a human serum albumin (HSA) stationary phase high-pressure liquid chromatography (HPLC) has been successfully used for the past few years to characterize the interactions between HSA and new substrates. Immobilized HSA conserves the binding properties of the protein in solution, allowing fast and reliable analyses of binding interactions. Nevertheless, clear evidence that all binding mechanisms of HSA-HPLC are pharmacologically relevant is so far lacking. In particular, non-stoichiometric interactions of injected ligands with stationary phase components such as silica and the amino acid medium (other than protein binding areas) might interfere with the correlation between chromatographic retention and HSA binding. Here we present a quantitative method to distinguish between the molecular interactions of a ligand with binding areas of potential pharmacological interest and other, non-saturable binding mechanisms. Such a method, based on HPLC same-ligand displacement, is simple and reliable, as confirmed by in situ protein denaturation. Consequently, we were able to distinguish between different types of competitions detected in the co-binding of two drugs to HSA.
Circular dichroism studies with adenosine deaminase from calf intestinal mucosa are described. Addition of purine riboside, a competitive inhibitor of the enzyme, does not cause modification of mean residue ellipticity in the CD spectra in the region between 250 and 185 nm, but increases markedly the ellipticity in the 300-250 nm region. The data are consistent with the view that a conformational change involving aromatic amino acid residues occurs upon binding of purine riboside to adenosine binding site of adenosine deaminase.
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