Interaction of tRNA with antitumor polyamine analogues

C. N. N'soukpoé-Kossi, A. Ahmed Ouameur, T. Thomas, Thekkumkat Thomas, H. A. Tajmir-Riahi

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

We studied the interaction between tRNA and three polyamine analogues (1,11-diamino-4,8-diazaundecane .HCl (333), 3,7,11,15-tetrazaheptadecane.HCl (BE-333), and 3,7,11,15,19-pentazahenicosane.HCl (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 (PO2 -) 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 K333 = 2.8 (±0.5) × 104, KBE-333 = 3.7 (±0.7) × 104, KBE-3333 = 4.0 (±0.9) × 104, Kspm = 8.7 (±0.9) × 105, Kspd = 6.1 (±0.7 × 105, and Kput = 1.0 (±0.3) × 105 mol/L. tRNA remained in the A-family conformation; however, it aggregated at high polyamine analogue concentrations.

Original languageEnglish (US)
Pages (from-to)621-630
Number of pages10
JournalBiochemistry and Cell Biology
Volume87
Issue number4
DOIs
StatePublished - Aug 1 2009

Fingerprint

Polyamines
Transfer RNA
Biogenic Polyamines
Uracil
Guanine
Adenine
Phosphates
Fourier Transform Infrared Spectroscopy
Sugars
Conformations
Catalytic Domain

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Keywords

  • Binding constant
  • DNA aggregation
  • DNA stability
  • FTIR spectroscopy
  • Polyamines
  • Preferential binding site
  • tRNA

Cite this

N'soukpoé-Kossi, C. N., Ahmed Ouameur, A., Thomas, T., Thomas, T., & Tajmir-Riahi, H. A. (2009). Interaction of tRNA with antitumor polyamine analogues. Biochemistry and Cell Biology, 87(4), 621-630. https://doi.org/10.1139/O09-036
N'soukpoé-Kossi, C. N. ; Ahmed Ouameur, A. ; Thomas, T. ; Thomas, Thekkumkat ; Tajmir-Riahi, H. A. / Interaction of tRNA with antitumor polyamine analogues. In: Biochemistry and Cell Biology. 2009 ; Vol. 87, No. 4. pp. 621-630.
@article{85d5296f6b6d44cba187357334f0a529,
title = "Interaction of tRNA with antitumor polyamine analogues",
abstract = "We studied the interaction between tRNA and three polyamine analogues (1,11-diamino-4,8-diazaundecane .HCl (333), 3,7,11,15-tetrazaheptadecane.HCl (BE-333), and 3,7,11,15,19-pentazahenicosane.HCl (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 (PO2 -) 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 K333 = 2.8 (±0.5) × 104, KBE-333 = 3.7 (±0.7) × 104, KBE-3333 = 4.0 (±0.9) × 104, Kspm = 8.7 (±0.9) × 105, Kspd = 6.1 (±0.7 × 105, and Kput = 1.0 (±0.3) × 105 mol/L. tRNA remained in the A-family conformation; however, it aggregated at high polyamine analogue concentrations.",
keywords = "Binding constant, DNA aggregation, DNA stability, FTIR spectroscopy, Polyamines, Preferential binding site, tRNA",
author = "N'soukpo{\'e}-Kossi, {C. N.} and {Ahmed Ouameur}, A. and T. Thomas and Thekkumkat Thomas and Tajmir-Riahi, {H. A.}",
year = "2009",
month = "8",
day = "1",
doi = "https://doi.org/10.1139/O09-036",
language = "English (US)",
volume = "87",
pages = "621--630",
journal = "Biochemistry and Cell Biology",
issn = "0829-8211",
publisher = "National Research Council of Canada",
number = "4",

}

N'soukpoé-Kossi, CN, Ahmed Ouameur, A, Thomas, T, Thomas, T & Tajmir-Riahi, HA 2009, 'Interaction of tRNA with antitumor polyamine analogues', Biochemistry and Cell Biology, vol. 87, no. 4, pp. 621-630. https://doi.org/10.1139/O09-036

Interaction of tRNA with antitumor polyamine analogues. / N'soukpoé-Kossi, C. N.; Ahmed Ouameur, A.; Thomas, T.; Thomas, Thekkumkat; Tajmir-Riahi, H. A.

In: Biochemistry and Cell Biology, Vol. 87, No. 4, 01.08.2009, p. 621-630.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Interaction of tRNA with antitumor polyamine analogues

AU - N'soukpoé-Kossi, C. N.

AU - Ahmed Ouameur, A.

AU - Thomas, T.

AU - Thomas, Thekkumkat

AU - Tajmir-Riahi, H. A.

PY - 2009/8/1

Y1 - 2009/8/1

N2 - We studied the interaction between tRNA and three polyamine analogues (1,11-diamino-4,8-diazaundecane .HCl (333), 3,7,11,15-tetrazaheptadecane.HCl (BE-333), and 3,7,11,15,19-pentazahenicosane.HCl (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 (PO2 -) 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 K333 = 2.8 (±0.5) × 104, KBE-333 = 3.7 (±0.7) × 104, KBE-3333 = 4.0 (±0.9) × 104, Kspm = 8.7 (±0.9) × 105, Kspd = 6.1 (±0.7 × 105, and Kput = 1.0 (±0.3) × 105 mol/L. tRNA remained in the A-family conformation; however, it aggregated at high polyamine analogue concentrations.

AB - We studied the interaction between tRNA and three polyamine analogues (1,11-diamino-4,8-diazaundecane .HCl (333), 3,7,11,15-tetrazaheptadecane.HCl (BE-333), and 3,7,11,15,19-pentazahenicosane.HCl (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 (PO2 -) 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 K333 = 2.8 (±0.5) × 104, KBE-333 = 3.7 (±0.7) × 104, KBE-3333 = 4.0 (±0.9) × 104, Kspm = 8.7 (±0.9) × 105, Kspd = 6.1 (±0.7 × 105, and Kput = 1.0 (±0.3) × 105 mol/L. tRNA remained in the A-family conformation; however, it aggregated at high polyamine analogue concentrations.

KW - Binding constant

KW - DNA aggregation

KW - DNA stability

KW - FTIR spectroscopy

KW - Polyamines

KW - Preferential binding site

KW - tRNA

UR - http://www.scopus.com/inward/record.url?scp=68049097880&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=68049097880&partnerID=8YFLogxK

U2 - https://doi.org/10.1139/O09-036

DO - https://doi.org/10.1139/O09-036

M3 - Article

C2 - 19767825

VL - 87

SP - 621

EP - 630

JO - Biochemistry and Cell Biology

JF - Biochemistry and Cell Biology

SN - 0829-8211

IS - 4

ER -

N'soukpoé-Kossi CN, Ahmed Ouameur A, Thomas T, Thomas T, Tajmir-Riahi HA. Interaction of tRNA with antitumor polyamine analogues. Biochemistry and Cell Biology. 2009 Aug 1;87(4):621-630. https://doi.org/10.1139/O09-036