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New paper: Redirecting RiPP Biosynthetic Enzymes to Proteins and Backbone-Modified Substrates

Led by C-GEM postdoc Josh Walker, this paper describes the installation of thiazoline and thiazole backbone modifications in peptides and proteins, including those containing non-natural monomers. This work is a collaboration between the Schepartz and Francis labs, with contributions from Noah Hamlish, Avery Tytla, and… Read More »New paper: Redirecting RiPP Biosynthetic Enzymes to Proteins and Backbone-Modified Substrates

New paper: genetic code expansion with high yield and exceptional fidelity

Genetic code expansion has tremendous potential to revolutionize peptide, protein, and protein-like therapeutics through the strategic substitution of non-canonical amino acids – or even more exotic monomers – to improve functional diversity, pharmacodynamics, produce antibody-drug conjugates, or even generate novel macrocycles. In all of these… Read More »New paper: genetic code expansion with high yield and exceptional fidelity