Peptide conjugation to an in vitro-selected DNA ligand improves enzyme inhibition.
收藏PubMed Central1995-11-21 更新2026-05-02 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC40567/
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资源简介：
An in vitro selection technique was used to identify a specific high-affinity DNA ligand targeted to human neutrophil elastase (HNE). 1H NMR data and a comparative analysis of the selected sequences suggest that the DNA folds into a G-quartet structure with duplexed ends. The high-affinity binding DNA alone did not inhibit the enzymatic activity of HNE. The DNA was covalently attached to a tetrapeptide, N-methoxysuccinyl-Ala-Ala-Pro-Val, that is a weak competitive inhibitor of HNE. HNE was inhibited by this DNA-peptide conjugate nearly five orders of magnitude more effectively than by the peptide alone. These results demonstrate that in vitro-selected nucleic acids can be used as a vehicle for molecular delivery. IMAGES:
提供机构：
National Academy of Sciences
创建时间：
1995-11-21
