We report the binding of testo and testo-Pt(II) complexes (testosterone derivatives) with tRNA in aqueous solution at physiological pH. Thermodynamic parameter Δ -8 to -3 (kJ mol), Δ 35 to 18 (J molK) and Δ -14 to -13 (kJ mol) and other spectroscopic results showed drug-tRNA binding occurs via ionic contacts with testo-Pt(II) forming more stable tRNA complexes in comparison to testo: -Pt(II)-tRNA= 3.2 (± 0.9) × 10 M > -tRNA= 2.1 (± 0.7) × 10 M. Molecular modeling showed multiple binding sites for testo and testo-Pt(II) on tRNA molecule. Some of the useful molecular descriptors are calculated. Major structural changes were observed for biopolymers upon drug complexation, while tRNA remains in the A-family structures.
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