Influence of solvent composition on the mechanical properties of arterial elastin
- 1 March 1990
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 29 (4-5) , 729-735
- https://doi.org/10.1002/bip.360290407
Abstract
We have investigated the effects of changes in solution composition on the mechanical properties of rings of arterial elastin. The time course of force equilibration at constant strain following a change in the composition of the bathing solution was measured. Both the force developed during slow extension and force relaxation following rapid straining were also measured in each of the test solutions. The results are difficult to summarize because all of the primitive quantities measured—sample dimension, slope of the force‐extension curve, force overshoot and time of relaxation—as well as the derived quantities such as elastic modulus changed in different and apparently uncorrelated ways. Changes in pH and ionic composition of the bathing solution had small effects consistent with the low fixed charge density of elastin. Solutions of glucose, sucrose, and ethylene glycol had larger effects consistent with changes in hydrophobic interactions. The viscosity of the solution that penetrated the intrafibrillar space of the elastin appeared to be a major determinant of the dynamic response.This publication has 20 references indexed in Scilit:
- The Uptake of Ions and Neutral Solutes by the Artery and by Artery Wall PreparationsConnective Tissue Research, 1988
- Extrafibrillar proteoglycans osmotically regulate the molecular packing of collagen in cartilageBiochimica et Biophysica Acta (BBA) - General Subjects, 1986
- Protein glycosylation and the pathogenesis of atherosclerosisMetabolism, 1985
- Elastin as a random‐network elastomer: A mechanical and optical analysis of single elastin fibersBiopolymers, 1981
- Dynamic mechanical properties of elastinBiopolymers, 1979
- Hydrophobic interaction and a model for the elasticity of elastinBiopolymers, 1978
- Effect of Hydrophobic Elastin Ligands on the Stress-Strain Properties of Elastin FibersConnective Tissue Research, 1976
- Calcium ion-binding study on α-elastinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1974
- Additional evidence for the binding of calcium ions to elastin at neutral sitesCalcified Tissue International, 1974
- Hydrophobic bonding and accessible surface area in proteinsNature, 1974