AUTHOR=Faravelli Giulia , Mondani Valentina , Mangione P. Patrizia , Raimondi Sara , Marchese Loredana , Lavatelli Francesca , Stoppini Monica , Corazza Alessandra , Canetti Diana , Verona Guglielmo , Obici Laura , Taylor Graham W. , Gillmore Julian D. , Giorgetti Sofia , Bellotti Vittorio TITLE=Amyloid Formation by Globular Proteins: The Need to Narrow the Gap Between in Vitro and in Vivo Mechanisms JOURNAL=Frontiers in Molecular Biosciences VOLUME=9 YEAR=2022 URL=https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2022.830006 DOI=10.3389/fmolb.2022.830006 ISSN=2296-889X ABSTRACT=
The globular to fibrillar transition of proteins represents a key pathogenic event in the development of amyloid diseases. Although systemic amyloidoses share the common characteristic of amyloid deposition in the extracellular matrix, they are clinically heterogeneous as the affected organs may vary. The observation that precursors of amyloid fibrils derived from circulating globular plasma proteins led to huge efforts in trying to elucidate the structural events determining the protein metamorphosis from their globular to fibrillar state. Whereas the process of metamorphosis has inspired poets and writers from Ovid to Kafka, protein metamorphism is a more recent concept. It is an ideal metaphor in biochemistry for studying the protein folding paradigm and investigating determinants of folding dynamics. Although we have learned how to transform both normal and pathogenic globular proteins into fibrillar polymers