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 stabilizing 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 language | English |
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Article number | 4093 |
Number of pages | 27 |
Journal | International Journal of Molecular Sciences |
Volume | 22 |
Issue number | 8 |
DOIs | |
Publication status | Published - 15 Apr 2021 |
User-Defined Keywords
- Aptamer
- Binding affinity
- Interaction feature
- Modification strategy
- Structure