Location of multiple binding sites for testo and testo-Pt(II) with tRNA

被引:7
作者
Chanphai, P. [1 ]
Ouellette, V. [1 ]
Mandal, S. [2 ]
Mandal, S. K. [3 ]
Berube, G. [1 ]
Tajmir-Riahi, H. A. [1 ]
机构
[1] Univ Quebec Trois Rivieres, Dept Chem Biochem & Phys, CP 500, Trois Rivieres, PQ, Canada
[2] Univ Manitoba, Rady Fac Hlth Sci, Dept Physiol & Pathophysiol,Albrechtsen Res Ctr, Inst Cardiovasc Sci,St Boniface Hosp,Coll Med, Winnipeg, MB, Canada
[3] Mem Univ Newfoundland, Fac Med, Coll North Atlantic, St John, NF, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
tRNA; testo-Pt(II); conjugation; spectroscopy; docking; LONG NONCODING RNAS; CISPLATIN; DNA; TESTOSTERONE; INSIGHTS; DIMERS;
D O I
10.1080/07391102.2018.1541142
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We report the binding of testo and testo-Pt(II) complexes (testosterone derivatives) with tRNA in aqueous solution at physiological pH. Thermodynamic parameter Delta H-0 -8 to -3 (kJ mol(-1)), Delta S-0 35 to 18 (J mol(-1)K(-1)) and Delta G(0) -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: K-testo-Pt(II)-tRNA= 3.2 (+/- 0.9) x 10(5) M-1 > K-testo-tRNA= 2.1 (+/- 0.7) x 10(5) 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.
引用
收藏
页码:4133 / 4139
页数:7
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