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Calorimetric characterization of 2′,3′-dideoxyinosine water solution

Stability and interaction with human serum albumin

Journal of Thermal Analysis and Calorimetry
Authors: Katarzyna Michalik, Zofia Drzazga, and Anna Michnik

Abstract  

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.

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Abstract  

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 volumesV ϕ and heat capacitiesC . 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 ofC Pϕ3,tr which depended on the concentration of Gly-Gly were observed.

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