UC Santa Barbara

Protein aggregation can impact the product quality of pharmaceutical drugs in terms of efficacy, safety, and immunogenicity leading to economic and technical problems for biotechnology and pharmaceutical companies. Furthermore, protein aggregation can lead to the onset of a variety of diseases including amyloidosis, prion diseases, and other protein deposition disorders. To combat these issues, we investigated the potential of aptamers to prevent protein aggregation within our model, modified fluorescent protein. We have identified and successfully demonstrated that the previous selected AP3 aptamer has a high affinity for not only green fluorescent protein (GFP), but also to emerald GFP with a KD of 199 nM. Our work has successfully demonstrated that protein aggregation can be inhibited upon binding of RNA aptamers.