Guthrie Stroh

The pharmaceutical landscape has recently seen increasing divergence from the dichotomy of small molecules (<900 Da) vs. monoclonal antibodies (~150 kDa). Splitting this size disparity are certain classes of ribosomally synthesized and post-translationally modified peptides (RiPPs). Some RiPPs are highly thermostable and protease-resistant, thereby possessing the potential to serve as lead molecules in a new regime of evolvable, re-programmable, and orally-bioavailable peptidic medicines. My research aims to explore this proposition by developing high throughput RiPP screening assays and by leveraging machine learning algorithms to engineer peptides with novel bioactivities.