Development of tailored amino acids for diverse biochemical and material functions
Application in creating proteins with properties unachievable with natural amino acids
Tryptophan (Trp) fluorescence is a powerful way to study protein structure, dynamics, and function, thanks to its strong emission and sensitivity to its surroundings. However, Trp’s photophysics can be challenging. By substituting Trp with fluorinated aromatic amino acids, we can suppress natural fluorescence (4-fluorotryptophan) or greatly enhance it (5-fluorotryptophan). These same substitutions also fine-tune protein stability - either reducing or strengthening it - providing precise control over a protein’s behavior (Original article: Biochemistry; 1999, 38(33),10649-59; doi: 10.1021/bi990580g).
Protein Translation Systems
Pioneering orthogonal translation systems to synthesize entirely novel biopolymers
Reprogrammed protein translation is a method that lets us interpret the original genetic message differently, effectively altering the universal “genetic code”—the fundamental language of life on Earth! (Original article: Angew Chem Int Ed Engl. 2010, 26, 49(32), 5446-50; doi: 10.1002/anie.201000439)
Environmental and Medical Biotechnology
Designing enzymes for plastic degradation and waste management
Creating synthetic materials and adhesives for wound healing and tissue regeneration (see “Safe, Sticky Solutions”)
Safe, Sticky Solutions: Mussel-Inspired Bio-Glues from Genetically Engineered Cells
Artificial life can be seen as a technology ideal for the development and production of wet adhesion biomaterials that could revolutionize in vivo tissue or wound healing and bone regeneration technologies. In this way, genetically isolated synthetic cells, safely confined to labs, serve as platforms for developing wet-adhesion biomaterials that could transform in vivo tissue repair and bone regeneration. Inspired by mussel adhesive proteins using L-Dopa for wet adhesion, we introduced a light-activatable oNB-Dopa revealing catechol groups upon irradiation. To add antimicrobial properties, we engineered Nisin A with clickable side chains, enabling conjugation via click chemistry. Our elastin-like peptide (ELP) fused to GFP also incorporates L-Dopa or oNB-Dopa co-translationally through orthogonal pairs and can be further modified by metabolic engineering and click chemistry (Original articles: ChemBioChem 2019, 20 (17), 2163-2190; doi: 10.1002/cbic.201900030; Front. Microbiol. 2018, 9, e657; doi: 10.3389/fmicb.2018.00657; Front. Microbiol. 2017, 8, e124; doi: 10.3389/fmicb.2017.00124).
