On the molecular and supramolecular structure of elastin
| Autor: | A. M. Tamburro, Valeria Guantieri, A. De Stradis, D. Daga Gordini |
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| Jazyk: | angličtina |
| Rok vydání: | 1994 |
| Předmět: | |
| Zdroj: | PROPERTIES AND CHEMISTRY OF BIOMOLECULAR SYSTEM, pp. 389–403. Dordrecht: Kluwer Academic Publishers, 1994 info:cnr-pdr/source/autori:A.M. TAMBURRO; D. DAGA GORDINI; V. GUANTIERI; DE STRADIS A/titolo:On the molecular and supramolecular structure of elastin/titolo_volume:PROPERTIES AND CHEMISTRY OF BIOMOLECULAR SYSTEM/curatori_volume:/editore: /anno:1994 Topics in Molecular Organization and Engineering ISBN: 9789401043533 |
| Popis: | Elastin, the protein responsible for elasticity in most tissues of vertebrates, displays peculiar aminoacid composition and primary sequence. Actually, about 90% of aminoacid residues are apolar, and quite unusual cross-links (desmosine and isodesmosine) [1] and many repetitive sequences are present [2–6]. the mature, insoluble protein originates from a soluble precursor called tropoelastin by posttranslational cross-linking. In recent years gene analysis has revealed the primary sequence of tropoelastins from different sources, such as the human [2], bovine [3],, chick [4], and murine [5] species. While these findings have considerably deepened our understanding of the elastin system, there are still several unanswered questions: is elastin a “classical” elastomer according to Flory theory [7] or not ?, is the supramolecular, fibrous structure of the protein determined by some preferred molecular conformation? Other questions concern the possible biological role played by specific sequences of elastin. In particular, tropoelastin itself and some peptides such as VGVAPG, AGVPGFGVG, GFGVGAGVP and GFGVG have been shown to possess chemotactic activity towards fibroblasts [8-10]. Interestingly, one of these peptides is a fragmentation product of elastase attack. Therefore, one wonders whether they could play a physiological and/or pathological role. in addition, recent studies have evidenced several immunogenic regions of the proteins including the chemotactic sequence VGVAPG [8,9]. Interestingly, this sequence is also chemotactic for certain tumor cell lines such as the M 27 line of the Lewis lung carcinoma [11]. One current approach toward elastin structure-function relationships has been based on investigations concerning synthetic models and fragments of the protein. As mentioned, the primary sequence of elastins is characterized by many repetitive sequences. The repetition, when cosidered in a statistical sense, can be found at different scales: at the lowest scale XGG and XPG (X=A, V, L, I) sequences are very frequently found, at the highest scale the entire protein has been interpreted as the repetition of few particular domains [4]. Given that, one can reasonably approach the problem of elastin structure through the synthesis of appropriate “monomers” and repeating polypeptides (polimers). |
| Databáze: | OpenAIRE |
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