期刊
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
卷 11, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fcell.2023.1091809
关键词
aptamer; chemical modification; high affinity; non-covalent bonding; interaction
Nucleic acid aptamers are single-stranded DNA or RNA fragments that can specifically recognize targets. However, natural aptamers composed of 4 naturally occurring nucleosides often have inferior binding affinity compared to antibodies. To address this, various high-affinity modification strategies have been developed, such as nucleobase modifications, fluorine modifications, structural alteration modifications, phosphate modifications, and extended alphabets. These modifications enhance the non-covalent bonding between the modified aptamers and target proteins, resulting in significantly improved affinity. This review provides an overview of these high-affinity modification strategies and their effects on the pharmacodynamic properties of aptamers.
Nucleic acid aptamers are ssDNA or ssRNA fragments that specifically recognize targets. However, the pharmacodynamic properties of natural aptamers consisting of 4 naturally occurring nucleosides (A, G, C, T/U) are generally restricted for inferior binding affinity than the cognate antibodies. The development of high-affinity modification strategies has attracted extensive attention in aptamer applications. Chemically modified aptamers with stable three-dimensional shapes can tightly interact with the target proteins via enhanced non-covalent bonding, possibly resulting in hundreds of affinity enhancements. This review overviewed high-affinity modification strategies used in aptamers, including nucleobase modifications, fluorine modifications (2 '-fluoro nucleic acid, 2 '-fluoro arabino nucleic acid, 2 ',2 '-difluoro nucleic acid), structural alteration modifications (locked nucleic acid, unlocked nucleic acid), phosphate modifications (phosphorothioates, phosphorodithioates), and extended alphabets. The review emphasized how these high-affinity modifications function in effect as the interactions with target proteins, thereby refining the pharmacodynamic properties of aptamers.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据