Dendrimer and Peptide Based Excipients for the Attenuation of Protein Aggregation


This technology is a protein-stabilizing compound that has applications in protein therapeutic manufacturing and commercial protein/enzyme synthesis.

Problem Addressed

Protein-based therapeutics are one of the fastest growing pharmaceutical sectors, and recombinant proteins are widely used in fields including biotechnology research, agriculture, and food production. A major challenge in manufacturing recombinant proteins is preventing formation of aggregates. Protein aggregates are non-functional and can even be toxic in vivo, therefore it is imperative that the aggregate formation is minimized and residual aggregates removed. Optimizing production and storage conditions to prevent aggregation is currently time consuming, costly, and requires trial and error testing due to the diversity of protein structures, therefore, there is a need to develop a universal anti-aggregation solution.


This technology universally stabilizes proteins to prevent aggregation using polyamidoamine (PAMAM) dendrimers with a guanidinium surface. The PAMAM dendrimers are an order of magnitude more efficient at preventing protein aggregation than other commonly used excipients such as sucrose and arginine hydrochloride. Aggregation rate is one of the primary determinants of the shelf life of protein therapeutics, and the use of PAMAM dendrimers extends the shelf life proteins formulations to nearly 5 months at room temperature compared to under 2 weeks for traditional excipients. In addition to use as an excipient, PAMAM dendrimers can be used to prevent aggregation in the high temperature reaction conditions needed to make recombinant proteins, thereby increasing yield and preventing aggregates from clogging machinery.


  • Universal anti-aggregation additive for recombinant protein synthesis and storage
  • Decreases aggregation rate by an order of magnitude compared to standard excipients
  • Reduces costs associated with developing protein synthesis conditions
  • Increases shelf life of recombinant proteins
  • Improves protein yield by reducing aggregation during manufacturing
  • Simple removal if desired