A Purdue University College of Pharmacy Researcher has found a way to manufacture important chemical structures required as catalysts to help form chemical structures that can stabilize certain medications in a more controlled manner.
Severin Schneebeli, associate professor in the Department of Industrial and Molecular Pharmaceutics (IMPH), had his research, “Kinetically Controlled Synthesis of Rotaxane Geometric Isomers,” published in Chem Sci. This study unveiled a pioneering method for creating mechanically interlocked molecular structures with unprecedented precision, advancing the fields of biomedicine and pharmaceutical science.
The research involved a team of collaborators, including Dr. Ke Xu, an IMPH postdoctoral scholar; Mica Schenkelberg, a Purdue Chemistry graduate; and Nils Balegamire, an IMPH PhD student. The study’s first co-author is Dr. Dillon McCarthy, a former PhD student in Schneebeli’s lab during his previous tenure at the University of Vermont.
The team’s work provides a new way for rings and molecular chains to interlock, which offers potential breakthroughs in the manufacturing and design of biomedically significant polymers, Schneebeli said.
“The reactions discovered represent an artificial self-correcting system, where desired structures are amplified while undesired ones are removed,” he said. “This high selectivity provides essential groundwork for safely producing polymers that stabilize peptide and protein drugs.”
This study is part of Schneebeli’s National Science Foundation CAREER Award, which supports early career faculty who have the potential to serve as academic role models in research and education and to lead advances in the mission of their department or organization.
Schneebeli’s CAREER Award focus is on finding better ways to control polymer growth for advanced biomedically useful polymers. His team’s findings could enable improved drug delivery systems and catalysts for creating well-defined polymers, vital for stabilizing and delivering protein drugs to targeted organs.
“We were initially surprised by the high selectivity observed in these reactions,” he said. “This was an initial serendipitous discovery, which we ultimately understood and were able to improve further as described in the paper.”
Schneebeli’s overall research program is focused on supramolecular and computational protein biotechnology with three major themes:
- Development of new supramolecular tools and catalysts for barcode-free selection and directed evolution of peptide and protein drugs.
- Innovation of accurate multiscale computational models with constant pH capability needed to elucidate the membrane permeation mechanism of new oral peptide drug formulations.
- Computational design of improved peptide libraries with a focus on advancing the delivery and formulation properties of peptide therapeutics.
