Interaction of tRNA with antitumor polyamine analogues

• Published in: Biochemistry and cell biology Vol. 87; no. 4; pp. 621 - 630
• Main Authors: N'soukpoé-Kossi, C. N, Ahmed Ouameur, A, Thomas, T, Thomas, T. J, Tajmir-Riahi, H. A
• Format: Journal Article
• Language: English
• Published: Canada NRC Research Press 01.08.2009; Canadian Science Publishing NRC Research Press
• Subjects: agrégation d'ADN; Antineoplastic Agents - chemistry; ARNt; binding constant; Binding sites; Biochemistry; Biogenic Polyamines - chemistry; Chemical properties; Circular Dichroism; constante de liaison; DNA aggregation; DNA stability; Evaluation; FTIR spectroscopy; Health aspects; Nucleic Acid Conformation; Pharmacokinetics; Polyamines; preferential binding site; Protein binding; RNA, Transfer - chemistry; site de liaison préférentiel; Spectrophotometry, Ultraviolet; spectroscopie IRTF; Spectroscopy, Fourier Transform Infrared; Spectrum analysis; stabilité d'ADN; Studies; Transfer RNA; tRNA; Canada
• ISSN: 0829-8211; 1208-6002
• DOI: 10.1139/O09-036

We studied the interaction between tRNA and three polyamine analogues (1,11-diamino-4,8-diazaundecane·4HCl (333), 3,7,11,15-tetrazaheptadecane·4HCl (BE-333), and 3,7,11,15,19-pentazahenicosane·5HCl (BE-3333)) using FTIR, UV-visible, and CD spectroscopic methods. Spectroscopic evidence showed that polyamine analogues bound tRNA via guanine N7, adenine, uracil O2, and the backbone phosphate (PO 2 - ) groups, while the most reactive sites for biogenic polyamines were guanine N7/O6, adenine N7, uracil O2, and sugar 2′-OH groups as well as the backbone phosphate group. The binding constants of polyamine analogue - tRNA recognition were lower than those of the biogenic polyamine - tRNA complexes, with K 333 = 2.8 (±0.5) × 10 4 , K BE-333 = 3.7 (±0.7) × 10 4 , K BE-3333 = 4.0 (±0.9) × 10 4 , K spm = 8.7 (±0.9) × 10 5 , K spd = 6.1 (±0.7) × 10 5 , and K put = 1.0 (±0.3) × 10 5 mol/L. tRNA remained in the A-family conformation;; however, it aggregated at high polyamine analogue concentrations.