Original scientific paper

https://doi.org/10.5562/cca2430

Solution Structure of a Prion Protein Aptamer Analogue

Špela Medic ; Slovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia
Peter Podbevšek orcid.org/0000-0002-2563-4507 ; Slovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia;EN-FIST Centre of Excellence, Trg Osvobodilne fronte 13, SI-1000 Ljubljana, Slovenia
Janez Plavec orcid.org/0000-0003-1570-8602 ; Slovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia;EN-FIST Centre of Excellence, Trg Osvobodilne fronte 13, SI-1000 Ljubljana, Slovenia;Faculty of Chemistry and Chemical Technology, University of Ljubljana, A

Abstract

It has previously been shown that r(GGA)4 folds into a G-quadruplex structure, which binds to the normal cellular form of the prion protein (PrPC) with high affinity. The current study utilizes CD and NMR spectroscopy to show that a dimeric parallel G-quadruplex structure is formed by r(GGA)2 in a KCl solution. Each r[(GGA)2]2 G-quadruplex unit exhibits two G-quartets, one of which is hydro- gen bonded to two additional adenines forming a hexade. Through stacking of hexade planes, two
G-quadruplex units interact with each other and form a symmetric dimer, r[(GGA)2]4. The topolo¬gy of r[(GGA)2]4 is in agreement with the fold of r[(GGA)4]2, however, subtle differences are found in the region responsible for PrPC binding.

Keywords

G-quadruplex; RNA; aptamer; NMR; GGA repeat; prion protein

Hrčak ID:

131524

URI

https://hrcak.srce.hr/131524

Publication date:

22.12.2014.

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