Development of aptameric affinity ligands specific to human plasma coagulation factor VIII using SEC-SELEX

Vahidi, Hossein; Nafissi-varcheh, Nastaran; Kazemi, Bahram; Aboofazeli, Reza; Shahhosseini, Soraya; Tabarzad, Maryam

doi:10.22037/ijpr.2017.2059

Development of aptameric affinity ligands specific to human plasma coagulation factor VIII using SEC-SELEX

Document Type : Research article

Authors

¹ Department of Pharmaceutical Biotechnology, School of Pharmacy, Shahid Beheshti University of Medical Sciences, Tehran, Iran.

² Cellular and Molecular Biology Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran. Biotechnology Department, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.

³ Department of Pharmaceutics, School of Pharmacy, Shahid Beheshti University of Medical Sciences, Tehran, Iran.

⁴ Department of Pharmaceutical Chemistry, School of Pharmacy, Shahid Beheshti University of Medical Sciences, Tehran, Iran.

⁵ Protein Technology Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran

10.22037/ijpr.2017.2059

Abstract

Protein specific aptamers are highly applicable affinity ligands in different fields of research and clinical applications. They have been developed against various targets, in particular, bio-macromolecules such as proteins. Among human proteins, the coagulation factors are the most attractive targets for aptamer selection and their specific aptamers had valuable characteristics in therapeutic and analytical applications. In this study, a plasma derived coagulation factor VIII was considered as the protein target for DNA aptamer selection using size exclusion chromatography-SELEX. Potential aptameric oligonucleotides with high affinity and specificity were achieved during eight rounds of selection. Binding affinity constant of selected aptamer and aptameric enriched pool were in nanomolar range that was comparable to monoclonal antibodies. Further improvement studies can result in aptamers that are more promising as an industrial affinity ligand for the purification of anti-hemophilia factor from plasma source.

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