Supramolecular Amyloid-like Assembly of the Polypeptide Sequence Coded by Exon 30 of Human Tropoelastin

Tamburro, Antonio Mario; Pepe, Antonietta; Bochicchio, Brigida; Quaglino, Daniela; Ronchetti, Ivonne Pasquali

doi:10.1074/jbc.m411617200

Cited by 94 publications

(90 citation statements)

References 58 publications

(53 reference statements)

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“…Each fibril was found to be composed of many polypeptide molecules (Fig. 2b), which is in line with previous reports suggesting that amyloid-like fibrils are likely to originate from extensive self-interactions of elemental cross ␤-structures (19). We also were able to observe fine structural features of the fibrils, such as the characteristic helical twist.…”

Section: Resultssupporting

confidence: 78%

“…It may be possible that the aggregation into such well defined, nanoordered assemblies represents a state of an efficient minimal energy arrangement of polypeptide chains (15)(16)(17). Recent results have shown that fibrillar structures similar to amyloid fibrils are formed by sequences like poly(XGlyGlyYGly) (X, Y ϭ Val, Leu, or Ala), which are highly repeated in the hydrophobic domains of elastin (18,19).…”

Section: Charge Transport and Intrinsic Fluorescence In Amyloid-like mentioning

confidence: 99%

See 1 more Smart Citation

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Mercato

Pompa²,

Maruccio³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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204

203

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Section: Resultssupporting

confidence: 78%

Section: Charge Transport and Intrinsic Fluorescence In Amyloid-like mentioning

confidence: 99%

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Mercato

Pompa²,

Maruccio³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

204

203

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“…3B) (17,29). Exceptions to this were EP20-P12-P12, EP20-24-P6N, and EP20-P6N-P6N, which all contained prominent peaks at 1625 cm Ϫ1 usually associated with ␤-sheet (17,25,27), suggesting that these polypeptides were relatively susceptible to the formation of such ␤-structures.…”

Section: Distribution Of Proline Residues In Hydrophobic Sequencesmentioning

confidence: 99%

Proline Periodicity Modulates the Self-assembly Properties of Elastin-like Polypeptides

Muiznieks

Keeley

2010

Journal of Biological Chemistry

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Elastin is a self-assembling protein of the extracellular matrix that provides tissues with elastic extensibility and recoil. The monomeric precursor, tropoelastin, is highly hydrophobic yet remains substantially disordered and flexible in solution, due in large part to a high combined threshold of proline and glycine residues within hydrophobic sequences. In fact, proline-poor elastin-like sequences are known to form amyloidlike fibrils, rich in ␤-structure, from solution. On this basis, it is clear that hydrophobic elastin sequences are in general optimized to avoid an amyloid fate. However, a small number of hydrophobic domains near the C terminus of tropoelastin are substantially depleted of proline residues. Here we investigated the specific contribution of proline number and spacing to the structure and self-assembly propensities of elastin-like polypeptides. Increasing the spacing between proline residues significantly decreased the ability of polypeptides to reversibly self-associate. Real-time imaging of the assembly process revealed the presence of smaller colloidal droplets that displayed enhanced propensity to cluster into dense networks. Structural characterization showed that these aggregates were enriched in ␤-structure but unable to bind thioflavin-T. These data strongly support a model where proline-poor regions of the elastin monomer provide a unique contribution to assembly and suggest a role for localized ␤-sheet in mediating self-assembly interactions.Elastin is the extracellular matrix protein responsible for the elasticity of vertebrate arterial vessels, connective tissues, lung, and skin. Elastin resilience is afforded by the formation of insoluble fibers, the first step of which involves the selfalignment of elastin monomers, tropoelastin, in a temperature-induced transition known as coacervation, through the association of hydrophobic domains (1, 2). Although highly (Ͼ75%) non-polar in character, tropoelastin remains predominantly monomeric and structurally disordered in solution (3-5) and critically, retains substantial backbone hydration and flexibility even when assembled (6) and cross-linked into mature, polymeric elastic arrays (7-13).Maintenance of structural heterogeneity and dynamics of the elastin backbone is achieved in large part by a high proportional composition of both proline (14%) and glycine (35%) residues within hydrophobic sequences (6, 14). These residues are commonly arranged into repeated motifs based on recurring sequence elements such as PGV and GVA. This includes a seven-fold tandem PGVGVA repeat in domain 24 of the native human elastin sequence (15). Contrary to enhancing coacervation or elastomeric properties, the multiple substitution of glycine residues for prolines within tandem repeat sequences (e.g. PGVGVA to GGVGVA) results in the formation of amyloid-like fibrils, rich in ␤-structure, from solution (6, 14). These structures are conformationally more restricted than native elastomeric sequences as a result of the tighter packing of residues into extended...

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“…Tropoelastin forms coacervates at temperatures above its LCST, and it is thought that this behavior is partially responsible for elastin's ability to form fibrils [31][32][33]203]. In addition, Tamburro et al have conducted many studies on the structures of tropoelastin, and their results provide further insight into the role secondary structure has on to the self-assembly of elastin fibers [204][205][206][207].…”

Section: Human Tropoelastin-based Polypeptidesmentioning

confidence: 99%

Peptide-based biopolymers in biomedicine and biotechnology

Chow

Nunalee

Lim

et al. 2008

Materials Science and Engineering: R: Reports

280

231

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Peptides are emerging as a new class of biomaterials due to their unique chemical, physical, and biological properties. The development of peptide-based biomaterials is driven by the convergence of protein engineering and macromolecular self-assembly. This review covers the basic principles, applications, and prospects of peptide-based biomaterials. We focus on both chemically synthesized and genetically encoded peptides, including poly-amino acids, elastin-like polypeptides, silk-like polymers and other biopolymers based on repetitive peptide motifs. Applications of these engineered biomolecules in protein purification, controlled drug delivery, tissue engineering, and biosurface engineering are discussed.

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Supramolecular Amyloid-like Assembly of the Polypeptide Sequence Coded by Exon 30 of Human Tropoelastin

Cited by 94 publications

References 58 publications

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Proline Periodicity Modulates the Self-assembly Properties of Elastin-like Polypeptides

Peptide-based biopolymers in biomedicine and biotechnology

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