Temperature dependence of length of elastin and its polypentapeptide

Urry, Dan W.; Haynes, Bryant; Harris, R. D.

doi:10.1016/s0006-291x(86)80236-4

Cited by 37 publications

(40 citation statements)

References 11 publications

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“…That the microscopic order of this remarkable biopolymer influences a macroscopic observable is made further evident by considering the thermal properties of elastin. Over the temperature range of 20–40 °C elastin undergoes a hydrophobic collapse [9–14]; a process by which the hydration of nonpolar solutes are opposed by the entropy of water ordering near 25 °C, [15]. The hydrophobic collapse of the protein near this temperature is understood to reduce the entropy of the protein.…”

Section: Introductionmentioning

confidence: 99%

“…For example, experimental studies of polypentapeptides have demonstrated that elastin undergoes an inverse temperature transition near 20 °C [9–11,16]. Both a γ -irradiated elastin mimetic polypentapeptide, as well as bovine nuchal ligament elastin have been observed to decrease in length dramatically upon increasing the temperature from 20 °C to 40 °C.…”

Section: Introductionmentioning

confidence: 99%

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Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR

Sun¹,

Boutis²

2010

Journal of Magnetic Resonance

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The anisotropic motion of tightly bound waters of hydration in bovine nuchal ligament elastin has been studied by deuterium Double Quantum Filtered (DQF) NMR. The experiments have allowed for a direct measurement of the degree of anisotropy within pores of elastin over a time scale ranging from 100 μs to 30 ms, corresponding to a tortuous spatial displacement ranging from 0.2 to 7 μm. We studied the anisotropic motion of deuterium nuclei in D2O hydrated elastin over a temperature of −15 °C to 37 °C and in solvents with varying dielectric constants. Our experimental measurements of the residual quadrupolar interaction as a function of temperature are correlated to the existing notion of hydrophobic collapse near 20 °C.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR

Sun¹,

Boutis²

2010

Journal of Magnetic Resonance

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“…The first conformational studies on elastomeric sequences were performed on some repetitive sequences of elastin, such as (LGGVG)n, [17][18][19] (VPGVG)n [20][21][22] and independent domains containing quasi-repetitive sequences.…”

Section: Introductionmentioning

confidence: 99%

Investigating by CD the molecular mechanism of elasticity of elastomeric proteins

2008

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Elastomeric proteins are widespread in the animal kingdom, and their main function is to confer elasticity and resilience to organs and tissues. Besides common functional properties, elastomeric proteins share a common sequence design. They are usually constituted by repetitive sequences with a high content of glycine residues. From a conformational point of view, all the elastomeric proteins since now analyzed show a dynamic equilibria between folded (mainly beta-turns) and extended (polyproline II and beta-strands) conformations that could be at the origin of the high entropy of the relaxed state. As a matter of fact, elastin, lamprin, abductin, as well as the PEVK domain of titin share the same conformational ensemble, thus pointing to a common molecular mechanism as the origin of elasticity. CD spectroscopy represents the proper spectroscopic technique to be used overall because of its particular sensitivity to the presence of PPII structure. Its use in the molecular studies of elastin, abductin, and lamprin as well as the recently analyzed protein resilin will be presented.

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“…The custom-built stress/strain apparatus was as previously described (17,19). Elastomers were equilibrated in PBS: 370C for X20-polypentapeptide at pH 7.4, 370C for X20-4%-Glu-PPP at pH 2.1, and 50'C for X20-4%-Glu-PPP at pH 4.5.…”

Section: Methodsmentioning

confidence: 99%

“…Those physical characterizations include (i) self-assembly studies, in which the polypeptide is found to assemble into several-micrometer-diameter fibers composed of fibrils that in turn are composed of approximately 50-A-diameter filaments (8-10); (ii) circular dichroism and Raman spectroscopy, in which the polypeptide chains within the coacervate are seen to have a repeating p-turn conformation (11,12); (iii) nuclear Overhauser effect studies, which demonstrate the specific hydrophobic side chain associations (ref. 13, D.W.U., D. K. Chang, R. Krishna, D. H. Huang, T. L. Trapane, and K.U.P., unpublished data); (iv) NMR studies, which show a decrease in backbone mobility as the temperature is raised through the transition under conditions of constant composition (14,15); (v) dielectric relaxation studies, which show the development of an intense, localized, Debye-type relaxation near 10 MHz requiring the development of a regular dynamic backbone conformation (16); (vi) elastomer length studies, in which the elastomer shortens to less than 45% of its low-temperature length when the temperature is raised from 20'C to 40'C (17); and (vii) studies of slow thermal denaturation at 80'C in which the circular dichroism indicates the loss of order (4), composition studies show a dramatic expulsion of water to a new composition of 68% peptide and 32% water by weight (4), and, for the elastomer, there is a decrease in length and loss of elastic modulus (ref. 18 and references therein).…”

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confidence: 99%

Mechanochemical coupling in synthetic polypeptides by modulation of an inverse temperature transition.

Urry

Haynes

Zhang

et al. 1988

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

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For the polypentapeptide of elastin, (L-Val-L-Pro-Gly-L-Val-Gly The polypeptide ofinterest is the polypentapeptide of elastin, (L-Val-L-Pro-Gly-L-Val-Gly)n, discovered in porcine elastin (1, 2). In bovine elastin, the longest sequence between lysine residues, which can form the cross-links, is 72 residues; for a continuous and unsubstituted sequence of 57 residues, this is the polypentapeptide (3). The synthetic polypentapeptide is soluble in water in all proportions below 250C, but when the temperature is raised above 250C, aggregation occurs, followed by settling and phase separation. At 40'C, the more dense viscoelastic phase is 38% peptide and 62% water by weight (4 In thermoelasticity studies when the synthetic elastomer is stretched and held at fixed length and the temperature is raised through the transition range from 20'C to 40'C, there is a dramatic increase in elastomeric force (5). Above 40TC, however, in a plot of In(elastomeric force/temperature) versus temperature the slope is nearly 0 (5); these data, along with composition studies that show a near constant coacervate volume and composition in the 40-60'C temperature range (4), provide one basis for indicating that the elastomeric force is dominantly entropic in origin. A most instructive demonstration that this transition, centered near 30'C, in which elastomeric force develops is an inverse temperature transition is given when the more hydrophobic polypentapeptide (L-Ile-L-Pro-Gly-L-Val-Gly),,-i.e., the [Ilel]polypentapeptide-is similarly cross-linked and studied (18). For this more hydrophobic elastomeric matrix, the temperature of the transition for development of elastomeric force in a thermoAbbreviations: 4%-Glu-PPP, elastin polypentapeptide in which 4% of the residues are glutamic acid; X2-, crosslinked at 20 Mrad y-irradiation. *With the exception of two reports from one other laboratory (6, 7), to our knowledge, the only synthesis and physical characterizations of the sequential polypeptides of elastin and their analogs are due to the work of, and collaborations involving, this laboratory. Because of this, an unseemly high proportion of the references in this article will necessarily be to our own publications. 3407The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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Temperature dependence of length of elastin and its polypentapeptide

Cited by 37 publications

References 11 publications

Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR

Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR

Investigating by CD the molecular mechanism of elasticity of elastomeric proteins

Mechanochemical coupling in synthetic polypeptides by modulation of an inverse temperature transition.

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