Authors:Katarzyna Michalik, Zofia Drzazga, and Anna Michnik
A study of 2′,3′-dideoxyinosine (ddI) stability and its interaction with human serum albumin (HSA) was carried out by differential
scanning microcalorimetry DSC. Scan rate dependent and irreversible endothermic thermal degradation of ddI was analyzed with
use of kinetic approach. Observed process could be interpreted in terms of simple first-order one step kinetic model. Moreover
it was shown that ddI bound weakly to the human serum albumin and stabilized this protein.
Authors:B. Golankiewicz, A. Zielenkiewicz, J. Zeidler, and W. Zielenkiewicz
2′3′-dideoxyinosine (ddI) and 2′3′-dideoxyadenosine (ddA) are known to exhibit relatively selective activityvs. HIV strains in cell cultures and low toxicityin vivo; ddI has been approved for the treatment of HIV infection in humans. It is therefore interesting to determine the thermodynamic
properties of aqueous solutions of these compounds. For this purpose, we determined their apparent molar volumesVϕ and heat capacitiesCPϕ. The preliminary measurements of interaction of these compounds with peptides were made. The volume and molar heat capacities
of transfer of ddI and ddA from aqueous solutions to glycyl-glycine (Gly-Gly) ones were calculated. For both compounds the
significant values ofCPϕ3,tr which depended on the concentration of Gly-Gly were observed.