Evidence for Order in the Structure of α-Elastin

Mammi, M.; Gotte, L.; Pezzin, G.

doi:10.1038/220371b0

Cited by 56 publications

(25 citation statements)

References 9 publications

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“…3, FTIR spectra of elastin hydrogel showed two main peaks at 1535 cm À1 , and 1655 cm À1 corresponding to the amide II and amide I bands, respectively. Similar peaks were observed for bovine elastin and k-elastin [25], human elastin [26], bovine tropoelastin [27], a-elastin [28,29], two elastinlike poly(pentapeptides) [30], and synthetic elastin hydrogels [31]. The FTIR spectra of PCL showed a main peak at 1725 cm À1 attributed to C]O stretching; this peak was also observed in previous studies for electrospun PCL samples [32].…”

Section: Ftir Analysis On Compositessupporting

confidence: 81%

The effect of elastin on chondrocyte adhesion and proliferation on poly (ɛ-caprolactone)/elastin composites

et al. 2011

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Section: Ftir Analysis On Compositessupporting

confidence: 81%

The effect of elastin on chondrocyte adhesion and proliferation on poly (ɛ-caprolactone)/elastin composites

et al. 2011

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“…Measurements of circular dichroism suggest (20) that solubilized elastin undergoes a marked conformational change on coacervation. Similar, but less marked, changes occur on addition of ethanol to aqueous solutions (21). Recent studies in this laboratory, to be reported elsewhere, show that the same conformational change occurs in trifluoroethanol containing 2.5% water and in trifluoroethanol containing 2.5% water plus 4% trifluoroacetic acid.…”

Section: Probable Glycine-containing Sequences and Associated Neutralmentioning

confidence: 58%

Neutral Sites for Calcium Ion Binding to Elastin and Collagen: A Charge Neutralization Theory for Calcification and Its Relationship to Atherosclerosis

Urry

1971

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

160

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Neutral, uncharged binding sites for calcium ions are proposed for elastin and collagen. The sites utilize, particularly from a conformational viewpoint, the most striking feature of the amino acid composition, that is, the high glycine content. Glycines favor the formation of B-turns and associated conformations that are known, from studies on ion-transporting antibiotics, to interact with cations. By analogy with certain antibiotics, which are uncharged polypeptides and depsipeptides that bind cations by coordination with neutral acyl oxygens, it is proposed that calcium-ion binding also utilizes uncharged coordinating groups, i.e., neutral sites, in the protein matrix. The protein matrix, which becomes positively charged by virtue of the bound calcium ions, attracts neutralizing phosphate and carbonate ions, which then allow further calcium ion binding. The driving force is, therefore, the affinity of calcium ions for the neutral nucleation sites.The charge neutralization theory of calcification suggests a fundamental role of organic anions, for example sulfated mucopolysaccharides, in regulating bone formation and in retardation of atherosclerosis. The proposed mechanism contains elements that tend to unify several theories on the pathogenesis of atherosclerosis.Elastin and collagen, particularly the former, exhibit a high affinity for calcium ions. There is, in fact, substantive argument, for example, that calcification of elastin is the initial process in the onset of the chronic disease arteriosclerosis; and the initiation of calcification is obviously an important process in bone and tooth formation as well as tendon insertion into bone and the emplacement of teeth. The significance of the initiation of calcification was emphasized by Urist (1) in his review of Selye's theory of calciphylaxis (2) when he stated

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“…Infrared absorption and circular dichroism (CD) studies on α-elastin, a heterogeneous product derived from acid hydrolysis of elastin [11], indicated that solubilized elastin has a predominantly disordered structure. Nuclear magnetic resonance studies reveal that the majority of backbone carbonyl carbon atoms in elastin-based polypeptides are highly mobile [12].…”

Section: Fundamental Understanding Of Tropoelastinmentioning

confidence: 99%

Tropoelastin: A versatile, bioactive assembly module

et al. 2014

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Elastin provides structural integrity, biological cues and persistent elasticity to a range of important tissues including the vasculature and lungs. Its critical importance to normal physiology makes it a desirable component of biomaterials that seek to repair or replace these tissues. The recent availability of large quantities of the highly purified elastin monomer, tropoelastin, have allowed for a thorough characterization of the mechanical and biological mechanisms underpinning the benefits of mature elastin. While tropoelastin is a flexible molecule, a combination of optical and structural analyses has defined key regions of the molecule that directly contribute to the elastomeric properties and control the cell interactions of the protein. Insights into the structure and behavior of tropoelastin have translated into increasingly sophisticated elastin-like biomaterials, evolving from classically manufactured hydrogels and fibers to new forms, stabilized in the absence of incorporated cross-linkers. Tropoelastin is also compatible with synthetic and natural co-polymers, expanding the applications of its potential use beyond traditional elastin-rich tissues and facilitating finer control of biomaterial properties and the design of next-generation tailored bioactive materials.

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Evidence for Order in the Structure of α-Elastin

Cited by 56 publications

References 9 publications

The effect of elastin on chondrocyte adhesion and proliferation on poly (ɛ-caprolactone)/elastin composites

The effect of elastin on chondrocyte adhesion and proliferation on poly (ɛ-caprolactone)/elastin composites

Neutral Sites for Calcium Ion Binding to Elastin and Collagen: A Charge Neutralization Theory for Calcification and Its Relationship to Atherosclerosis

Tropoelastin: A versatile, bioactive assembly module

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