Nanostructured aptasensors for ricin detection and tumor therapy: exploring aptamer-protein interactions and...

Aptamers are distinctive single-stranded oligonucleotides derived through in vitro evolution, and exhibit exceptional ability in binding to target proteins. Structural modifications of aptamers can profoundly regulate their interactions with proteins, thereby influencing associated cellular behavior. Recent research focused on modulating aptamer-protein interaction in complex biological environments to regulate various biological processes. However, in such crowded conditions, aptamer conformation and stability are susceptible to nuclease degradation, which can impair stable binding to target. Ricin is recognized as a significant biological toxin protein, distinguished by its widespread availability, remarkable dissemination, and resilience including wide pH tolerance, remarkable thermostability, and solubility. RTA is an enzymatic subunit of ricin, that can inactivate approximately 2000 ribosomes per minute, rapidly halting protein synthesis, making it a powerful candidate for tumor therapy. By leveraging the potent cytotoxicity of ricin, coupled with the targeting precision of aptamers and the versatility of nanomaterials, a powerful approach emerges for both targeted tumor therapy and highly sensitive detection of ricin. Although there have been some insightful reports on aptamers applied in ricin detection, a systematic discussion remains limited. In this context, we provide an in-depth overview of techniques used to analyze aptamer-ricin interactions and explore the potential of ricin-aptamer interactions in clinical diagnosis.