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

J Biomol Struct Dyn. 2020 Jun;38(9):2686-2692. doi: 10.1080/07391102.2019.1642241. Epub 2019 Aug 8.

Abstract

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.

Keywords: G-quadruplex DNA; binding constant; binding mode; monovalent cation; porphyrin.

MeSH terms

  • Aptamers, Nucleotide*
  • Circular Dichroism
  • G-Quadruplexes*
  • Porphyrins*
  • Thrombin

Substances

  • Aptamers, Nucleotide
  • Porphyrins
  • thrombin aptamer
  • Thrombin