A method for fixation of elastin demonstrated by stress/strain characterization

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

doi:10.1016/s0006-291x(88)80335-8

Cited by 6 publications

(2 citation statements)

References 15 publications

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“…Still, that study demonstrates that there may be considerable flexibility in designing crosslinker/solvent combinations to achieve desired mechanical properties in bioprosthetic materials. If these techniques are to be extended to histological fixation, further work is necessary to compare these approaches to the use of potentially destructive, oxidative methods such as that described by Urry et al 27 using sodium hypochlorite.…”

Section: Table II Mechanical Test Results For Each Experimental Groupmentioning

confidence: 99%

Altered mechanical properties in aortic elastic tissue using glutaraldehyde/solvent solutions of various dielectric constant

Gratzer

Lee

1997

J. Biomed. Mater. Res.

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The extent to which elastic tissue can be crosslinked in aldehydes and the mechanism of such action is unresolved in the literature. We have used glutaraldehyde/solvent solutions of decreasing dielectric constant (phosphate buffer, methanol, 95% ethanol, n-propanol, n-butanol) to alter the mechanical properties of aortic elastic tissue obtained from autoclaved and CNBr-purified bovine aortae. Treated and untreated hoop samples were examined for stress-strain and stress relaxation behavior and for residual stress using opening angle experiments as per Fung. The extent of exogenous crosslinking was analyzed through amino acid analysis. Mechanical properties of autoclaved elastic tissue varied with dielectric constant in glutaraldehyde/solvent treatments; however, solvent treatment alone produced no effect. Extensibility decreased with decreasing dielectric constant while tensile modulus changed over a range from -2.4% (-0.86 kPa) for glutaraldehyde/buffer to +35.3% (+14.3 kPa) for glutaraldehyde/n-propanol (untreated-treated). Residual stress experiments similarly showed a systematic decrease in opening angle with decreasing dielectric constant. Differences ranged from 10.5 degrees for glutaraldehyde/buffer to 22.2 degrees for glutaraldehyde/n-butanol. Interestingly, purification of aortae with CNBr reduced the effects of glutaraldehyde/n-butanol treatment. We hypothesize that CNBr differentially degraded the elastin-associated microfibrillar proteins in aortic elastic tissue, thus producing the observed differences in mechanical behavior. The observed phenomena in this study may be attributed to the composite structure of elastic tissue: elastin and microfibrillar protein. During treatment, conformational changes in elastin facilitated by polar/nonpolar interactions occurred which then were "locked" in by glutaraldehyde crosslinking of the microfibrillar proteins. By this mechanism the increases in both stiffness and time-dependent behavior observed after treatment may be explained.

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Section: Table II Mechanical Test Results For Each Experimental Groupmentioning

confidence: 99%

Altered mechanical properties in aortic elastic tissue using glutaraldehyde/solvent solutions of various dielectric constant

Gratzer

Lee

1997

J. Biomed. Mater. Res.

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“…Oxidative stress seems a plausible explanation for this, i.e., increased mixing in the shaken solutions leads to thinner stationary boundary layers and better oxygen supply for oxidation-driven cross-linking processes. There is precedence for oxidative effects on the modulus of structural proteins: a brief treatment of elastin with 20% sodium hypochlorite increased the stiffness by a factor of eight (Urry et al, 1988). The modulus of tendon type I collagen increases with maturation (from 10 to 140 days) (Viidik et al, 1982) reflecting the oxidation-dependent formation of aldimine and aldol condensation crosslinks.…”

Section: Discussionmentioning

confidence: 99%

Oxidative Stress and the Mechanical Properties of Naturally Occurring Chimeric Collagen-Containing Fibers

Sun

Vaccaro

Waite

2001

Biophysical Journal

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The byssal threads of marine mussels are a fiber-reinforced composite material. Fibers are continuous, separated by matrix, and consist of chimeric collagens that encompass within the same primary protein structure domains corresponding to collagen, polyhistidine, and either elastin or dragline spider silk. The elastic modulus (stiffness) of the proximal portion of byssal threads was measured by cyclic stress-strain analysis at 50% extension. Before measurement, the threads were conditioned by various treatments, particularly agitation in aerated or nitrogen-sparged seawater. Stiffness can be permanently increased by more than two times, e.g., from 25 MPa to a maximum of 65 MPa, by simple agitation in aerated seawater. Much but not all of this stiffening can be prevented by agitation under nitrogen. Reversible strain stiffening would seem to be a useful adaptation to lower residual stresses arising from the deformation of two joined materials, i.e., distal and proximal portions with rather different elastic moduli. The permanent strain stiffening that characterizes proximal byssal threads subjected to oxidative stress is probably due to protein cross-linking. In the short term, this results in a stronger thread but at the expense of dynamic interactions between the molecules in the structure.

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