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- W2486944966 abstract "In this paper, we report the investigations, based on NMR, molecular modelling, CD measurements and electrophoresis, of thrombin binding aptamer (TBA) analogues containing an extra-residue at the 3'-end or at both the ends of the original TBA sequence, linked through 3'-3' or 5'-5' phosphodiester bonds. The data indicate that most of the modified aptamers investigated adopt chair-like G-quadruplex structures very similar to that of the TBA and that stacking interactions occur between the 3'-3' or 5'-5' extra residues and the deoxyguanosines of the upper G-tetrad. A comparison of the thermodynamic data of TBA-A and TBA-T containing a 3'-3' extra residue and their canonical versions clearly indicates that the 3'-3' phosphodiester bond is fundamental in endowing the modified aptamers with remarkably higher thermal stabilities than the original TBA." @default.
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- W2486944966 date "2016-01-01" @default.
- W2486944966 modified "2023-09-25" @default.
- W2486944966 title "Improved thrombin binding aptamer analogues containing inversion of polarity sites: structural effects of extra-residues at the ends" @default.
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- W2486944966 doi "https://doi.org/10.1039/c6ob00931j" @default.
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