Matt Webber (University of Notre Dame)


Location: 127 Nieuwland Science Hall

Abstract:  Using principles from supramolecular chemistry – that is, “chemistry beyond the molecule” – it is possible to create systems rationally designed at the molecular level that can address complexities associated with the deficiencies and dynamics of disease. The biological relevance of peptides, and the ability to precisely engineer supramolecular interactions through directional assembly and organized hydrogen bonding, enables the generation of platforms that can be utilized as functional therapeutic materials. These bio-inspired materials interface with biology and physiology in a mimetic and active way. Self-assembling peptides can be used to present potent bioactive signals at high density to mimic the function of angiogenic growth factors, or to prepare favorable niches for stem and progenitor cell therapeutics. Molecular interactions can additionally be leveraged to alter therapeutic dynamics and afford aspects of biologically relevant sensing in molecularly engineered protein therapies. Diabetes, and the complexities associated with glycemic control, present a significant engineering constraint in the design of therapies to recapitulate and replace the dynamics of native insulin signaling. Through covalent modification of insulin with molecular recognition motifs and aliphatic groups, the kinetics of insulin activity can be modulated by glucose-mediated dynamic covalent interactions, resulting in biomimetic insulin therapy. Alternatively, precise supramolecular host-guest interactions can be used to tune both the stability and activity of a broad suite of biopharmaceuticals, including insulin. In sum, these findings point to a new era of rationally engineered therapies rooted in predictable, biomimetic, tunable, and dynamic supramolecular interactions.

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