DNA aptamers targeting RNAP.

We present the first DNA aptamers designed to target the RNA polymerase (RNAP) of . Utilizing SELEX, we identified and examined aptamers, among which the R2 aptamer demonstrated high specificity and significant binding affinity for RNAP. R2 effectively captured RNAP, making it suitable for protein tandem purification and coating applications.

Aptamer-Assisted DNA SELEX: Dual-Site Targeting of a Single Protein.

Heterobivalent fusion aptamers that target a single protein show significant promise for studying protein-protein interactions. However, a major challenge is finding two distinct aptamers that can simultaneously recognize the same protein. In this study, we used a novel technique called Aptamer-Assisted DNA SELEX (AADS) to isolate two distinct aptamers capable of recognizing different sites on the programmed death-ligand 1 (PD-L1) protein.

Biotechnological Advances Utilizing Aptamers and Peptides Refining PD-L1 Targeting.

While monoclonal antibodies have shown success in cancer immunotherapy, their limitations prompt exploration of alternative approaches such as aptamers and peptides targeting programmed death ligand 1 (PD-L1). Despite the significance of these biotechnological tools, a comprehensive review encompassing both aptamers and peptides for PD-L1 targeting is lacking. Addressing this gap is crucial for consolidating recent advancements and insights in this field.

Aptamer-assisted phage display: enhancing checkpoint inhibition with a peptide and an aptamer targeting distinct sites on a single PD-L1 protein.

Utilizing a novel approach known as aptamer-assisted phage display (APD), we identified an anti-PD-L1 peptide, NV Pep, capable of simultaneous binding to PD-L1 alongside the DNA aptamer MJ5C. Combined inhibition using NV Pep and MJ5C demonstrated significant enhancement compared to individual ligands against the PD-1/PD-L1 interaction.

Ni aptamer: DNA mimic of His-tag to recognize Ni-NTA.

We introduced Ni Apt as the first aptamer with a characterized dissociation constant for recognizing Ni-NTA. Serving as a nucleic acid analog of the His-tag commonly employed for protein purification using Ni-NTA resin, Ni Apt displays a remarkable binding affinity ( = 106 nM) towards Ni-NTA. Furthermore, it can be eluted from the resin using imidazole or EDTA, similar to the removal of His-tag from Ni-NTA resin.

DNA aptamers inhibit SARS-CoV-2 spike-protein binding to hACE2 by an RBD- independent or dependent approach.

Nobody knows when the COVID-19 pandemic will end or when and where the next coronavirus will outbreak. Therefore, it is still necessary to develop SARS-CoV-2 inhibitors for different variants or even the new coronavirus. Since SARS-CoV-2 uses its surface spike-protein to recognize hACE2, mediating its entry into cells, ligands that can specifically recognize the spike-protein have the potential to prevent infection.

A universal DNA aptamer as an efficient inhibitor against spike-protein/hACE2 interactions.

A universal aptamer against spike-proteins of diverse SARS-CoV-2 variants was discovered DNA SELEX towards the wild-type (WT) spike-protein. This aptamer, A1C1, binds to the WT spike-protein or other variants of concern such as Delta and Omicron with low nanomolar affinities. A1C1 inhibited the interaction between hACE2 and various spike-proteins by 85-89%.