Abstract
We report the binding of testo and testo–Pt(II) complexes (testosterone derivatives) with tRNA in aqueous solution at physiological pH. Thermodynamic parameter ΔH0 −8 to −3 (kJ mol−1), ΔS0 35 to 18 (J mol−1K−1) and ΔG0 −14 to −13 (kJ mol−1) 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: Ktesto–Pt(II)–tRNA= 3.2 (± 0.9) × 105 M−1 > Ktesto-tRNA= 2.1 (± 0.7) × 105 M−1. 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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