title: Dissection of human tropoelastin: supramolecular organization of polypeptide sequences coded by particular exons.
abstract: Polypeptide sequences encoded by some exons of the human tropoelastin gene (EDP, elastin-derived peptide) have been analysed for their ability to coacervate and to self-assembly. The great majority of them were shown to form organized structures, but only a few were indeed able to coacervate. Negative staining and rotary shadowing transmission electron microscopy showed the polypeptides to adopt a variety of supramolecular organization, from filaments, as those typical of tropoelastin, to amyloid-like fibers. The results obtained gave significant insight to the possible roles played by specific polypeptide sequences of tropoelastin.
authors.affiliation: Department of Chemistry, Università della Basilicata, Via N. Sauro 85, 85100 Potenza, Italy.
authors.forename: Antonietta
authors.initials: A
authors.lastname: Pepe
authors.forename: Deanna
authors.initials: D
authors.lastname: Guerra
authors.forename: Brigida
authors.initials: B
authors.lastname: Bochicchio
authors.forename: Daniela
authors.initials: D
authors.lastname: Quaglino
authors.forename: Dealba
authors.initials: D
authors.lastname: Gheduzzi
authors.forename: Ivonne
authors.initials: I
authors.lastname: Pasquali Ronchetti
authors.forename: Antonio M
authors.initials: AM
authors.lastname: Tamburro
mesh_terms: D000682:Amyloid / Q000737:chemistry; D002942:Circular Dichroism; D004549:Elastin / Q000737:chemistry; D005091:Exons; D006801:Humans; D016014:Linear Models; D046911:Macromolecular Substances / Q000737:chemistry; D008854:Microscopy, Electron; D010455:Peptides / Q000737:chemistry; D013696:Temperature; D014333:Tropoelastin / Q000737:chemistry* / Q000235:genetics*
chemical_list: D000682:Amyloid; D046911:Macromolecular Substances; D010455:Peptides; D014333:Tropoelastin; D004549:Elastin