NDLI: Test of the librational entropy mechanism of elasticity of the polypentapeptide of elastin. Effect of introducing a methyl group at residue 5

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Test of the librational entropy mechanism of elasticity of the polypentapeptide of elastin. Effect of introducing a methyl group at residue 5

Content Provider	Royal Society of Chemistry (RSC)
Author	Urry, Dan W. Trapane, Tina L. Prasad, Kari U. Long, Marianna M.
Copyright Year	1983
Abstract	The polypentapeptide analogue, (Val1-Pro2-Gly3-Val4-Ala5)n, has been synthesized to test the proposed librational entropy mechanism of elasticity which is based on the polypentapeptide of elastin, (Val1-Pro2-Gly3-Val4-Gly5)n. The mechanism utilizes the motional capacities of the Val4-Gly5-Val1 segment of the elastin polypentapeptide in a β-spiral conformation in which the segment is suspended between β-turns. Proton and carbon-13 nuclear magnetic resonance spectroscopies have been used to verify purity and to demonstrate that the Pro2-Gly3β-turn is retained in the Ala5 analogue. In addition, the temperature profiles for aggregation are found to be similar for both polypentapeptides. Aggregation of the Ala5 analogue, however, so immobilizes the polypeptide as to give no carbon-13 nuclear magnetic resonance spectrum, whereas a broadened spectrum is observed for the aggregated state of the polypentapeptide of elastin. Scanning electron micrographs are used to compare the aggregated states of the two polymers. On settling, the polypentapeptide of elastin forms a smooth-appearing sheet whereas the addition of a methyl group at residue 5 results in a granular precipitate. In contrast to the elastomeric polypentapeptide of elastin, the Ala5 analogue, on cross-linking with γ-irradiation, simply fragments when stress/strain studies are attempted. Thus the introduction of a methyl group at residue 5 allows common conformational features to exist but destroys the elasticity in a manner consistent with the proposed librational entropy mechanism.The effects of this and other analogues of the polypentapeptide of elastin are discussed in terms of accessible configurations, and it is argued that by means of the β-spiral conformation the polypentapeptide of elastin provides a unique configurational entropy which is utilized to produce a new type of entropic elastomer.
Starting Page	853
Ending Page	868
Page Count	16
File Format	PDF
ISSN	03009599
Volume Number	79
Issue Number	4
Journal	Journal of the Chemical Society, Faraday Transactions 1
DOI	10.1039/F19837900853
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Elastin Methyl group Elastomer Proton Entropy Carbon-13 nuclear magnetic resonance Peptide
Content Type	Text
Resource Type	Article
Subject	Chemistry

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