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Merck
  • Binding mode of a cationic porphyrin to parallel and antiparallel thrombin binding aptamer G-quadruplex.

Binding mode of a cationic porphyrin to parallel and antiparallel thrombin binding aptamer G-quadruplex.

Journal of biomolecular structure & dynamics (2019-07-17)
Ha Young Cho, Young-Ae Lee, Ye Sol Oh, Gil Jun Lee, Yoon Jung Jang, Seog K Kim
摘要

The spectral properties of meso-tetrakis (N-methylpyridinium-4-yl)porphyrin (TMPyP) in the presence of parallel and antiparallel G-quadruplexes formed from a thrombin-binding aptamer G-quadruplex (5'-G3T2G3TGTG3T2G3) were investigated in this study. Red shift and hypochromism in the Soret absorption band of TMPyP were observed after binding to both parallel and antiparallel G-quadruplexes. The extent of changes in the absorption spectra were similar for both conformers. No circular dichroism spectrum was induced in the Soret region for both parallel and antiparallel G-quadruplexes. This is suggest that there is no or very weak interaction between electric transitions of nucleobases and porphyrin molecule. The accessibility of the neutral quencher I2 to the G-quadruplex-bound TMPyP was similar for both parallel and antiparallel G-quadruplexes. All these observations suggest that TMPyP was bound at the outside of the quadruplexes, and conceivably interacted with the phosphate group via a weak electrostatic interaction.Communicated by Ramaswamy H. Sarma.