Self-Illuminating Proteins Assemble Themselves Into Engineered Fibers, Show Potential as Therapeutic Agents Against Multiple Diseases

One of the major challenges in delivering drugs to the body is making sure that they stay in the area they are treating and continue to accurately deliver their payload. While innovations have been made in drug delivery, it is still a challenge to monitor them since it usually requires invasive procedures such as biopsies.

Protein-Engineered Fibers

To address this challenge, experts at New York University (NYU) Tandon School of Engineering have developed therapeutic proteins which can revolutionize the way we treat multiple diseases. Led by Chemical and Biomolecular Engineering professor Jin Kim Montclare, the research team created self-illuminating proteins which can assemble themselves into fibers. These biomaterials encapsulate and deliver drugs for a host of diseases, but scientists need to make sure that they continue to deliver therapeutics at the correct locations in the body for the required amount of time.

In the study "Protein-Engineered Fibers For Drug Encapsulation Traceable via 19F Magnetic Resonance", Montclare and her team created fluorinated biomaterials. Because of this fluorination, the materials can be monitored by simple FMRI scans which enables medical professionals to ensure that the drugs stay at the treatment areas through non-invasive imaging procedures.

The biomaterial is made up of natural proteins, but the researchers introduced the non-natural amino acid called trifluoroleucine. Since fluorine is rarely found in the human body, it enables the biomaterials to light up like a holiday display when the patient is put into an 19FMRI scan.

The fluorination technique also allows the materials to offer treatment for localized diseases which are far less invasive and less disruptive to monitor.

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Computational Design for Creating Hydrogel

The self-assembling proteins created by Montclare's team are only a subset of a study which involves the use of computational designs to create hydrogels from proteins. This experiment, in collaboration with Montclare's Ph.D. student Dustin Britton, is discussed in the paper "Computational Prediction of Coiled-Coil Protein Gelation Dynamics and Structure".

These hydrogels have different transition temperatures where they remain in gel state without being dissolved or unstable. The previous upper limit of gelation was around 17 degrees Celsius, which was suboptimal for biomedical applications since the hydrogel would melt upon approaching human body temperature. With the use of computationally designed proteins, Britton shifted this limit up to 33.6 degrees Celsius.

Due to its stability, the proteins designed by Britton and Montclare have the potential to be used for topical treatments, such as wound healing. Aside from increased heat tolerance, the new protein can also gel much faster than the earlier versions, making it more efficient and more useful for medical applications. Moreover, the gel has the same benefits of the proteins from the laboratory meant for internal use.

Britton's computer model does more than just designing the specific protein. As reported by Montclare, the field of protein engineered biomaterials has long been dominated by hypothetical designs that focus on trial and error. Britton's model was able to develop consistently successful gels by generating sequences with an extremely high success rate and making new proteins with new features for potential therapeutic applications.

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