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Structural Optimization and Interaction Study of a DNA Aptamer to L1 Cell Adhesion Molecule
Zhenhao Long1,2, Tao Bing1,3, Xiangru Zhang1,2
1Beijing National Laboratory for Molecular Sciences, Key Laboratory of Analytical Chemistry for Living Biosystems, CAS Research and Education Center for Excellence in Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, China.
International Journal of Molecular Sciences
|May 27, 2023
Summary
Researchers optimized DNA aptamers to strongly bind L1 cell adhesion molecule (L1CAM). These enhanced aptamers offer improved tools for L1CAM research and detection, aiding drug development.
Area of Science:
- Biochemistry
- Molecular Biology
- Biotechnology
Background:
- L1 cell adhesion molecule (L1CAM) is crucial for nervous system development and implicated in tumor progression.
- Development of specific ligands for L1CAM is essential for biomedical research and diagnostic applications.
Purpose of the Study:
- To optimize DNA aptamers for enhanced binding affinity to L1CAM.
- To elucidate the molecular interaction mechanism between aptamers and L1CAM.
- To provide guidance for developing L1CAM-targeting drugs and detection probes.
Main Methods:
- Sequence mutation and extension were employed to optimize DNA aptamer yly12 against L1CAM.
- Binding affinity was assessed at room temperature and 37 °C.
- Structural analysis revealed aptamer secondary structures and key binding regions.
- Domain-specific binding of aptamers to L1CAM was confirmed.
Main Results:
- Optimized aptamers (yly20, yly21) exhibited 10-24 fold stronger binding affinity for L1CAM.
- Aptamers adopted a hairpin structure with key nucleotides in loop I and adjacent areas.
- Stem I was identified as crucial for stabilizing the aptamer-L1CAM binding structure.
- The yly-series aptamers specifically bind to the Ig6 domain of L1CAM.
Conclusions:
- Optimized DNA aptamers demonstrate significantly enhanced binding to L1CAM.
- The study provides a detailed molecular understanding of aptamer-L1CAM interactions.
- These findings facilitate the design of novel L1CAM-based diagnostics and therapeutics.
