title: Investigating the role of (2S,4R)-4-hydroxyproline in elastin model peptides.
abstract: Post-translational modifications play a key role in defining the biological functions of proteins. Among them, the hydroxylation of proline producing the (2S,4R)-4-hydroxyproline (Hyp) is one of the most frequent modifications observed in vertebrates, being particularly abundant in the proteins of the extracellular matrix. In collagen, hydroxylation of proline plays a critical role, conferring the correct structure and mechanical strength to collagen fibers. In elastin, the exact role of this modification is not yet understood. Here we show that Hyp-containing elastin polypeptides have flexible molecular structures, analogously to proline-containing polypeptides. In turn, the self-assembly of the elastin peptides is significantly altered by the presence of Hyp, evidencing different supramolecular structures. Also the in vitro susceptibility to protease digestion is changed. These findings give a better insight into the elastic fiber formation and degradation processes in the extracellular matrix. Furthermore, our results could contribute in defining the subtle role of proline structural variants in the folding and self-assembly of elastin-inspired peptides, helping the rational design of elastin biomaterials.
authors.affiliation: Department of Science, University of Basilicata , Viale dell'Ateneo Lucano 10, 85100 Potenza, Italy.
authors.forename: Brigida
authors.initials: B
authors.lastname: Bochicchio
authors.forename: Alessandro
authors.initials: A
authors.lastname: Laurita
authors.forename: Andrea
authors.initials: A
authors.lastname: Heinz
authors.forename: Christian E H
authors.initials: CE
authors.lastname: Schmelzer
authors.forename: Antonietta
authors.initials: A
authors.lastname: Pepe
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D006801:Humans; D006900:Hydroxylation; D006909:Hydroxyproline / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008969:Molecular Sequence Data; D057139:Nanofibers / Q000737:chemistry / Q000648:ultrastructure; D010446:Peptide Fragments / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D014333:Tropoelastin / Q000737:chemistry* / Q000648:ultrastructure
chemical_list: D010446:Peptide Fragments; D014333:Tropoelastin; D006909:Hydroxyproline