Celebrating Professor George Barany's Half Century in Science
Published in Chemistry
Speakers
- Prof. Fernando Albericio Ph.D. — University of KwaZulu-Natal
- Prof. Elisar Barbar Ph.D. — Oregon State University
- Prof. Richard DiMarchi Ph.D. — Indiana University
- Prof. Carrie Haskell-Luevano Ph.D. — University of Minnesota
- Prof. Michael Weiss M.D., Ph.D. — Indiana University
- Prof. George Barany Ph.D. — University of Minnesota
Abstract
This seminar commemorates Professor George Barany’s five decades of contributions to peptide chemistry and related biomedical sciences, highlighting his pioneering work in orthogonal solid-phase peptide synthesis and its impact on protein folding, peptide therapeutics, and diabetes research. The presentations emphasize the integration of peptide synthesis with biophysical and biochemical analyses to elucidate protein folding pathways, exemplified by studies on bovine pancreatic trypsin inhibitor (BPTI). Barany’s synthetic strategies enabled the creation of site-specific analogs that revealed the folding core and partially folded intermediates, providing foundational insights into intrinsically disordered proteins (IDPs) and their functional ensembles. Advances in chemical synthesis facilitated the production of complex peptides and insulin analogs, overcoming challenges in folding efficiency and enabling industrial-scale manufacture of therapeutic proteins such as insulin and its derivatives. The seminar also addresses the application of native chemical ligation to generate clinical proinsulin variants, illuminating the molecular basis of toxic misfolding in monogenic diabetes syndromes and correlating folding efficiency with disease onset. Further, the development of novel peptide ligands targeting G-protein-coupled receptors (GPCRs) in neuroscience exemplifies the ongoing expansion of peptide-based drug discovery. Barany’s introduction of orthogonality in protecting group chemistry revolutionized peptide synthesis, allowing selective manipulations essential for complex molecule assembly. The collective work underscores the enduring significance of rigorous synthetic methodology combined with biophysical characterization in advancing peptide science, therapeutic innovation, and understanding of protein folding diseases, while also reflecting on mentorship, interdisciplinary collaboration, and the evolving landscape of macromolecular medicines.
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