Hydrophobic domains of human tropoelastin are able to aggregate in a variegated manner. Some aggregates have typical features of the whole protein while others show peculiar self-assembling profiles. Among these hydrophobic domains, an important role in the self-assembling properties of tropoelastin in vitro could be assigned to the peptide encoded by exon 26 of the human tropoelastin gene, that, although unstructured in solution, has great tendency to self-assemble in an ordered manner. The present report describes the aggregation properties of this hydrophobic domain of human tropoelastin analysed by different ultra-structural approaches. Transmission electron microscopy shows that the peptide is able to form different aggregation entities from short rods to very long and flexible fibers, depending on the temperature and on the incubation time. At a microm scale, very long fibers as well as fractal aggregation patterns were observed. Data show that the isolated domain encoded by exon 26 of the tropoelastin gene is able to aggregate in a manner very similar to the whole tropoelastin protein. The aggregation properties are due to the peculiar sequence of EX26, and not to its amino acid composition, as evidenced by the supramolecular analysis of a scrambled sequence of exon 26-coded domain of human tropoelastin, showing a quite different aggregation patterns. These findings confirm that specific sequences can play a driving role in the aggregation process of tropoelastin molecule, at least in vitro, and indicate exon 26-encoded domain among these sequences.

Exon 26-coded polypeptide: an isolated hydrophobic domain of human tropoelastin able to self-assemble in vitro / A., PEPE A; R., Flamis; Guerra, Deanna; Quaglino, Daniela; B., Bochicchio; Ronchetti, Ivonne; A. M., Tamburro. - In: MATRIX BIOLOGY. - ISSN 0945-053X. - STAMPA. - 27:5(2008), pp. 441-450. [10.1016/j.matbio.2008.02.006]

Exon 26-coded polypeptide: an isolated hydrophobic domain of human tropoelastin able to self-assemble in vitro.

GUERRA, Deanna;QUAGLINO, Daniela;RONCHETTI, Ivonne;
2008

Abstract

Hydrophobic domains of human tropoelastin are able to aggregate in a variegated manner. Some aggregates have typical features of the whole protein while others show peculiar self-assembling profiles. Among these hydrophobic domains, an important role in the self-assembling properties of tropoelastin in vitro could be assigned to the peptide encoded by exon 26 of the human tropoelastin gene, that, although unstructured in solution, has great tendency to self-assemble in an ordered manner. The present report describes the aggregation properties of this hydrophobic domain of human tropoelastin analysed by different ultra-structural approaches. Transmission electron microscopy shows that the peptide is able to form different aggregation entities from short rods to very long and flexible fibers, depending on the temperature and on the incubation time. At a microm scale, very long fibers as well as fractal aggregation patterns were observed. Data show that the isolated domain encoded by exon 26 of the tropoelastin gene is able to aggregate in a manner very similar to the whole tropoelastin protein. The aggregation properties are due to the peculiar sequence of EX26, and not to its amino acid composition, as evidenced by the supramolecular analysis of a scrambled sequence of exon 26-coded domain of human tropoelastin, showing a quite different aggregation patterns. These findings confirm that specific sequences can play a driving role in the aggregation process of tropoelastin molecule, at least in vitro, and indicate exon 26-encoded domain among these sequences.
27
5
441
450
Exon 26-coded polypeptide: an isolated hydrophobic domain of human tropoelastin able to self-assemble in vitro / A., PEPE A; R., Flamis; Guerra, Deanna; Quaglino, Daniela; B., Bochicchio; Ronchetti, Ivonne; A. M., Tamburro. - In: MATRIX BIOLOGY. - ISSN 0945-053X. - STAMPA. - 27:5(2008), pp. 441-450. [10.1016/j.matbio.2008.02.006]
A., PEPE A; R., Flamis; Guerra, Deanna; Quaglino, Daniela; B., Bochicchio; Ronchetti, Ivonne; A. M., Tamburro
File in questo prodotto:
Non ci sono file associati a questo prodotto.
Pubblicazioni consigliate

Caricamento pubblicazioni consigliate

Licenza Creative Commons
I metadati presenti in IRIS UNIMORE sono rilasciati con licenza Creative Commons CC0 1.0 Universal, mentre i file delle pubblicazioni sono rilasciati con licenza Attribuzione 4.0 Internazionale (CC BY 4.0), salvo diversa indicazione.
In caso di violazione di copyright, contattare Supporto Iris

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11380/611982
Citazioni
  • ???jsp.display-item.citation.pmc??? 4
  • Scopus 13
  • ???jsp.display-item.citation.isi??? 12
social impact