title: An aggregating elastin-like pentapeptide.
abstract: Synthetic VGGVG, a "monomeric" unit of the glycine-rich regions of elastin, has been investigated for its molecular and supramolecular properties. In aqueous solution the pentapeptide showed conformational features strongly concentration-dependent. CD and NMR studies suggested a partial unfolding on increasing the concentration. Electron microscopy, on the other hand, evidenced extensive aggregation of the pentapeptide yielding elastin-like supramolecular structures constituted either by twisted ropes or by banded fibrils.
authors.affiliation: Department of Chemistry, Universita' della Basilicata, Potenza, Italy.
authors.forename: M A
authors.initials: MA
authors.lastname: Morelli
authors.forename: M
authors.initials: M
authors.lastname: DeBiasi
authors.forename: A
authors.initials: A
authors.lastname: DeStradis
authors.forename: A M
authors.initials: AM
authors.lastname: Tamburro
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004549:Elastin / Q000737:chemistry* / Q000648:ultrastructure; D009682:Magnetic Resonance Spectroscopy; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D009842:Oligopeptides; D004549:Elastin