Structural biology for the molecular insight between aptamers and target proteins

Ning Zhang, Zihao Chen, Dingdong Liu, Hewen Jiang, Zong Kang Zhang, Aiping LYU, Bao Ting Zhang*, Yuanyuan YU, Ge Zhang

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

Abstract

Aptamers are promising therapeutic and diagnostic agents for various diseases due to their high affinity and specificity against target proteins. Structural determination in combination with multiple biochemical and biophysical methods could help to explore the interacting mechanism between aptamers and their targets. Regrettably, structural studies for aptamer–target interactions are still the bottleneck in this field, which are facing various difficulties. In this review, we first reviewed the methods for resolving structures of aptamer–protein complexes and for analyzing the interactions between aptamers and target proteins. We summarized the general features of the interacting nucleotides and residues involved in the interactions between aptamers and proteins. Challenges and perspectives in current methodologies were discussed. Approaches for determining the binding affinity between aptamers and target proteins as well as modification strategies for sta-bilizing the binding affinity of aptamers to target proteins were also reviewed. The review could help to understand how aptamers interact with their targets and how alterations such as chemical modifications in the structures affect the affinity and function of aptamers, which could facilitate the optimization and translation of aptamers‐based theranostics.

Original languageEnglish
Article number4093
JournalInternational Journal of Molecular Sciences
Volume22
Issue number8
DOIs
Publication statusPublished - 15 Apr 2021

Scopus Subject Areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

User-Defined Keywords

  • Aptamer
  • Binding affinity
  • Interaction feature
  • Modification strategy
  • Structure

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