Dr. van der Donk from the University of Illinois has characterized expression vectors and a family of proteases that are useful in removing affinity tags after...
Dr. van der Donk from the University of Illinois has characterized expression vectors and a family of proteases that are useful in removing affinity tags after protein expression. Affinity tag removal after protein expression is sometimes necessary for the protein of interest to be functional and active. However during this tag removal, some amino acids not native to the protein of interest can be left behind. Dr. van der Donk's invention eliminates the possibility of extraneous amino acids being left on the final protein product, which is an improvement over existing enzymatic tag removal techniques. This invention has identified a class of lanthipeptides, class II LanPs that show substrate specificity and can serve as efficient sequence-specific traceless proteases, expanding and advancing the current toolbox of proteases.
The general goal of Dr. van der Donk's research is to understand enzymatic transformations that are of environmental or pharmaceutical importance. The van der Donk lab utilizes both synthetic organic chemistry and molecular biology to reach this goal. Specifically, the lab uses genome mining strategies to discover new natural products, use microbiology and genomic tools to determine their mode of action, use chemical biology techniques to study their biosynthesis, and use synthetic chemistry to improve their activities and therapeutic properties.
Tremendous potential exists for helical polypeptides that are water soluble (ionic) and remain stable at physiological conditions, variable environmental conditions including pH fluctuations, temperature changes, and in the presence of denaturing agents for gene delivery and cell-membrane penetration over commercially available products.
Libraries of helical polypeptides are screened for desired traits, i.e. efficient gene transfection compared to standard transfection reagents.
