The effects of hydration on the dynamic mechanical properties of elastin

Lillie, Margo A.; Gosline, John M.

doi:10.1002/bip.360290805

Cited by 116 publications

(63 citation statements)

References 35 publications

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“…The plots are master curves that were constructed by combining the results of dynamic tests taken at a number of temperatures, using the timetemperature superposition principle for polymeric materials. This process allows one to predict the behaviour of elastin at a reference temperature, in this case 37°C, over a much broader range of frequencies than can be achieved in laboratory tests (Gosline & French 1979;Gosline 1980;Lillie & Gosline 1990). The logic is that decreasing temperature slows molecular motion, so that mechanical tests carried out at a temperature below the reference temperature will reveal the behaviour at frequencies above the test frequency, and vice versa.…”

Section: The Functional Design Of Rubber-like Proteinsmentioning

confidence: 99%

Elastic proteins: biological roles and mechanical properties

Gosline

Lillie

Carrington

et al. 2002

Phil. Trans. R. Soc. Lond. B

753

632

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The term 'elastic protein' applies to many structural proteins with diverse functions and mechanical properties so there is room for confusion about its meaning. Elastic implies the property of elasticity, or the ability to deform reversibly without loss of energy; so elastic proteins should have high resilience. Another meaning for elastic is 'stretchy', or the ability to be deformed to large strains with little force. Thus, elastic proteins should have low stiffness. The combination of high resilience, large strains and low stiffness is characteristic of rubber-like proteins (e.g. resilin and elastin) that function in the storage of elastic-strain energy. Other elastic proteins play very different roles and have very different properties. Collagen fibres provide exceptional energy storage capacity but are not very stretchy. Mussel byssus threads and spider dragline silks are also elastic proteins because, in spite of their considerable strength and stiffness, they are remarkably stretchy. The combination of strength and extensibility, together with low resilience, gives these materials an impressive resistance to fracture (i.e. toughness), a property that allows mussels to survive crashing waves and spiders to build exquisite aerial filters. Given this range of properties and functions, it is probable that elastic proteins will provide a wealth of chemical structures and elastic mechanisms that can be exploited in novel structural materials through biotechnology.

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Section: The Functional Design Of Rubber-like Proteinsmentioning

confidence: 99%

Elastic proteins: biological roles and mechanical properties

Gosline

Lillie

Carrington

et al. 2002

Phil. Trans. R. Soc. Lond. B

753

632

View full text Add to dashboard Cite

show abstract

“…Recently, water solvent was shown to act as a plasticizer for elastin (47), that is to say it enhances its mobility. Moreover, the action of solutes on the structure of elastin is indirect and seems to be mediated through its hydration shell (48).…”

Section: Fig 2 Nir Ft-r Spectrum Of Be In Powder In the Frequency Rmentioning

confidence: 99%

Bovine Elastin and κ-Elastin Secondary Structure Determination by Optical Spectroscopies

Debelle

Alix

Jacob

et al. 1995

Journal of Biological Chemistry

109

104

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Elastin is the macromolecular polymer of tropoelastin molecules responsible for the elastic properties of tissues. The understanding of its specific elasticity is uncertain because its structure is still unknown. Here, we report the first experimental quantitative determination of bovine elastin secondary structures as well as those of its corresponding soluble -elastin. Using circular dichroism and Fourier transform infrared and near infrared Fourier transform Raman spectroscopic data, we estimated the secondary structure contents of elastin to be ϳ10% ␣-helices, ϳ45% ␤-sheets, and ϳ45% undefined conformations. These values were very close to those we had previously determined for the free monomeric tropoelastin molecule, suggesting thus that elastin would be constituted of a closely packed assembly of globular ␤ structural class tropoelastin molecules crosslinked to form the elastic network (liquid drop model of elastin architecture). The presence of a strong hydration shell is demonstrated for elastin, and its possible contribution to elasticity is discussed.

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“…7 Several thermodynamic studies of elastin have indicated a strong dependence of the Young's modulus with the type of solvent and extent of hydration reinforcing the vital role of an aqueous environment that imparts its elasticity. [8][9][10] The strain dependence of the entropy and energy components of the stress for elastin samples in swelling equilibrium with different diluents has also been investigated. 11 It was shown that in water, the energetic component contributed $15% of the total stress.…”

mentioning

confidence: 99%

High resolutionq‐space imaging studies of water in elastin

et al. 2007

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We report on the direct measurement of the molecular diffusion coefficients of water confined to purified bovine nuchal ligament elastin by high resolution q‐space NMR imaging. The experimental data indicate that water trapped within an elastin fiber has two distinguishable molecular diffusion coefficients. The component with the slowest mobility has a diffusion coefficient on the order of 10−6 cm2/s that varies inversely with the diffusion time and is seen to reduce near 37°C. The component with higher mobility has a diffusion coefficient reminiscent of free water but is observed to also behave similarly at 37°C. From our experimental data we extract the surface‐to‐volume ratio of pores within elastin and associated changes as a function of temperature. © 2007 Wiley Periodicals, Inc. Biopolymers 87: 352–359, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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The effects of hydration on the dynamic mechanical properties of elastin

Cited by 116 publications

References 35 publications

Elastic proteins: biological roles and mechanical properties

Elastic proteins: biological roles and mechanical properties

Bovine Elastin and κ-Elastin Secondary Structure Determination by Optical Spectroscopies

High resolutionq‐space imaging studies of water in elastin

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