Aptamers targeting protein-specific glycosylation in tumor biomarkers: general selection, characterization and structural modeling
| Autor: | Dimas Suárez, Natalia Díaz, Noemí de-los-Santos-Álvarez, Ana Díaz-Fernández, Rebeca Miranda-Castro, M. Jesús Lobo-Castañón |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Glycan Glycosylation biology Chemistry Aptamer Peptide General Chemistry Computational biology 010402 general chemistry 01 natural sciences 0104 chemical sciences 03 medical and health sciences chemistry.chemical_compound Docking (molecular) biology.protein Cancer biomarkers Receptor Glycoprotein 030304 developmental biology |
| Zdroj: | Chemical Science RUO: Repositorio Institucional de la Universidad de Oviedo Universidad de Oviedo (UNIOVI) RUO. Repositorio Institucional de la Universidad de Oviedo instname |
| Popis: | Detecting specific protein glycoforms is attracting particular attention due to its potential to improve the performance of current cancer biomarkers. Although natural receptors such as lectins and antibodies have served as powerful tools for the detection of protein-bound glycans, the development of effective receptors able to integrate in the recognition both the glycan and peptide moieties is still challenging. Here we report a method for selecting aptamers toward the glycosylation site of a protein. It allows identification of an aptamer that binds with nM affinity to prostate-specific antigen, discriminating it from proteins with a similar glycosylation pattern. We also computationally predict the structure of the selected aptamer and characterize its complex with the glycoprotein by docking and molecular dynamics calculations, further supporting the binary recognition event. This study opens a new route for the identification of aptamers for the binary recognition of glycoproteins, useful for diagnostic and therapeutic applications. Binary recognition of the glycoprotein prostate specific antigen by aptamers: a tool for detecting aberrant glycosylation associated with cancer. |
| Databáze: | OpenAIRE |
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