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Dissection of Human Tropoelastin: Solution Structure, Dynamics and Self‐Assembly of the Exon 5 Peptide
Author(s) -
Bochicchio Brigida,
Floquet Nicolas,
Pepe Antonietta,
Alix Alain J. P.,
Tamburro Antonio M.
Publication year - 2004
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200305661
Subject(s) - tropoelastin , elastin , exon , peptide , biophysics , chemistry , molecular dynamics , crystallography , genetics , biochemistry , biology , gene , computational chemistry
The elastic properties of elastin have essentially been discussed in terms of dominant entropic components, with questions still remaining about whether the basic mechanism is compatible with the classical theory of rubber elasticity. A better understanding of the structure–function relationships in terms of the protein's elastic properties remains an important goal in elastin science. Recently, we succeeded in the exon‐by‐exon synthesis of all polypeptide sequences encoded by the so‐called hydrophobic exons and almost all of the cross‐linking exons of human tropoelastin. Among these, the peptide encoded by exon 5 (PGGLAGAGLGA) has been extensively studied by classical spectroscopic methods, such as CD and NMR spectroscopy, and by molecular dynamics simulations. The results obtained clearly evidenced a large flexibility of the polypeptide chain, which oscillates between rather extended conformations, such as PPII, and folded ones, such as β turns. At the supramolecular level, we obtained evidence by TEM that shows that the peptide encoded by exon 5 is able to self‐assemble in fibrillar structures, a result indicating that the “information” for self‐assembly is also contained within a small domain of tropoelastin.