Fluorescence spectroscopy study of single-stranded nucleic acid aptamer species against NS5 Zika virus

Zika virus (ZIKV) belongs to the Flaviviridae family and its recent outbreak and association with human diseases (e.g. neurological disorders) have raised global health concerns. The viral NS5 protein is the most conserved ZIKV protein, and is comprised of two domains, an N-terminal methyltransferase domain and an RNA-dependent RNA polymerase (RdRP) domain at the C-terminal end. The fact that viral NS5 is essential for viral replication but lacks a human counterpart makes NS5 an important target to be studied. Single-stranded ONA oligonucleotides aptamers can fold into unique three-dimensional conformations that recognize targets with high-specific and -affinity. This work aims to study single-stranded ONA aptamers displaying high affinity and specificity generated against ZIKV NS5 protein to be used in diagnostic platforms.