| Literature DB >> 33920991 |
Ning Zhang1,2, Zihao Chen1,2, Dingdong Liu2,3,4, Hewen Jiang1,2, Zong-Kang Zhang1,2, Aiping Lu2,3,4, Bao-Ting Zhang1,2, Yuanyuan Yu2,3,4, Ge Zhang2,3,4.
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.Entities:
Keywords: aptamer; binding affinity; interaction feature; modification strategy; structure
Year: 2021 PMID: 33920991 DOI: 10.3390/ijms22084093
Source DB: PubMed Journal: Int J Mol Sci ISSN: 1422-0067 Impact factor: 5.923