d-/l-Isothymidine incorporation in the core sequence of aptamer BC15 enhanced its binding affinity to the hnRNP A1 protein

Org Biomol Chem. 2018 Oct 17;16(40):7488-7497. doi: 10.1039/c8ob01454j.

Abstract

The heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) was reported to participate in the development of a variety of tumors. BC15 is a DNA aptamer targeting hnRNP A1. Firstly, through sequence truncation, we identified 31-mer sequence BC15-31 as the core sequence of BC15 with a strong binding affinity and high selectivity to the hnRNP A1 protein. Isothymidine (isoT) modification was then applied for the structural optimization of BC15-31, systematic modification and biological evaluation were carried out. Incorporation of isoT in the 1,3 sites at the 5'-end of BC15-31 can significantly enhance the protein affinity. Chemical modifications close to the 3'-end can greatly improve the stability of the aptamer. Furthermore, BC15-31 modified with isoT at both the 5'-end and 3'-end displayed an additive effect with enhanced bioactivity and stability at the same time. Our study strategy on BC15 provides a useful guideline for chemical modification and optimization of the aptamer for further clinical application.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • A549 Cells
  • Aptamers, Nucleotide / chemistry*
  • Aptamers, Nucleotide / genetics
  • Aptamers, Nucleotide / metabolism*
  • Aptamers, Nucleotide / pharmacology
  • Base Sequence
  • Cell Proliferation / drug effects
  • Hep G2 Cells
  • Heterogeneous Nuclear Ribonucleoprotein A1 / metabolism*
  • Humans
  • Protein Binding
  • Structure-Activity Relationship
  • Substrate Specificity
  • Thymidine / chemistry*

Substances

  • Aptamers, Nucleotide
  • Heterogeneous Nuclear Ribonucleoprotein A1
  • Thymidine