4.6 Article

Selection and Identification of an ssDNA Aptamer for Fibroblast Activation Protein

Journal

MOLECULES
Volume 28, Issue 4, Pages -

Publisher

MDPI
DOI: 10.3390/molecules28041682

Keywords

FAP; aptamer; CE; SELEX; cancer-associated fibroblasts

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As a transmembrane serine protease, fibroblast activation protein (FAP) is expressed on the surface of fibroblasts associated with various epithelial-derived malignancies. It plays a role in tumorigenesis, progression, and immunosuppression. This study selected five candidate aptamers for FAP using capillary electrophoresis-systematic evolution of ligands by exponential enrichment (CE-SELEX), and determined their secondary structures and affinity to FAP protein through CE-laser-induced fluorescence (LIF) method. The FAP aptamers, especially AptFAP-A4, showed potential for rapid tumor diagnosis and targeted therapy.
As a type II transmembrane serine protease, fibroblast activation protein (FAP) is specifically expressed on the surface of fibroblasts associated with a variety of epithelial-derived malignancies such as pancreatic cancer, breast cancer, and colon cancer. It participates in the processes of tumorigenesis, progression, and immunosuppression. FAP constitutes an important target for tumor treatment; however, the current studies on FAP are mainly related to structural characteristics, enzymatic properties, and biological functions, and aptamers of FAP have not been investigated. In this work, by using recombinant human FAP as the target, five candidate aptamers, which are AptFAP-A1, AptFAP-A2, AptFAP-A3, AptFAP-A4, and AptFAP-A5, were selected by capillary electrophoresis-systematic evolution of ligands by exponential enrichment (CE-SELEX), and their secondary structures were predicted to be mainly stem-loop. Moreover, the CE-laser-induced fluorescence (LIF) method was used to determine the equilibrium dissociation constant K-D values between the FAP protein and candidate aptamers, and the K-D value was in the low molar range. Finally, Cy5-labeled aptamers were co-incubated with human pancreatic cancer-associated fibroblasts highly expressing FAP protein, and confocal microscopy imaging showed that aptamer AptFAP-A4 had the highest affinities with the cells. The FAP aptamers screened in this study provide a promising direction for the development of rapid tumor diagnosis and targeted therapy.

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