学術雑誌論文

学術雑誌論文

text

Macromolecules. 2008, 41(19), p. 7203-7210

Chain dimensions and hydration behavior of collagen model peptides in aqueous solution: [Glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyproline]n, [Glycylprolyl-4(R)-hydroxyproline]n, and some related model peptides

American Chemical Society

英語

text

2008-09-04

https://doi.org/10.1021/ma800790w

Terao K., Mizuno K., Murashima M., et al. Chain dimensions and hydration behavior of collagen model peptides in aqueous solution: [Glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyproline]n, [Glycylprolyl-4(R)-hydroxyproline]n, and some related model peptides. Macromolecules, 41(19), 7203-7210, September 4, 2008. Copyright © 2008, American Chemical Society. https://doi.org/10.1021/ma800790w.

Small-angle X-ray scattering (SAXS), circular dichroism (CD), and density measurements were made on eight samples of collagen model peptides consisting of glycine (Gly), proline (Pro), and 4-(R)-hydroxyproline (Hyp), i.e., (Gly-Hyp-Hyp)n, (Gly-Pro-Hyp)n, (Gly-Hyp-Pro)n, and (Gly-Pro-Pro)n (n = 5 and 9) in pure water and in phosphate buffered saline at a wide range of temperatures between 4 and 75°C. A complete triple-helical structure was found only for (Gly-Hyp-Hyp)9 and (Gly-Pro-Hyp)9 at 15°C by SAXS and CD, and (Gly-Pro-Pro) 9 had a partially formed triple helix at 4°C. At 70°C or higher temperatures, all peptides are dispersed as monomeric chains in these solvents and have essentially the same radii of gyration as the literature values for denatured proteins with the equivalent number of amino acid residues, suggesting that the conformational entropy for the single chain of the collagen model peptides is almost independent of the imino acid content. Furthermore, the partial specific volume v̄ for (Gly-Hyp-Hyp)9 around the transition temperature decreases more gradually with decreasing temperature than that for (Gly-Hyp-Hyp)5. On the contrary, the temperature dependence of v̄ for (Gly-Pro-Hyp)n has the opposite tendency, indicating that the hydration number for the peptide (Gly-Pro-Hyp)9 increases with formation of the triple helix whereas that for the peptide (Gly-Hyp-Hyp)9 decreases. These results are consistent with the difference in the transition enthalpies reported previously [J. Biol. Chem. 2004, 279, 38072]. © 2008 American Chemical Society.

This document is the Accepted Manuscript version of a Published Work that appeared in final form in Macromolecules, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/ma800790w.

81835

Chain dimensions and hydration behavior of collagen model peptides in aqueous solution: [Glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyproline]n, [Glycylprolyl-4(R)-hydroxyproline]n, and some related model peptides

American Chemical Society

英語

2008-09-04

Macromolecules

41

19

7203

7210

https://doi.org/10.1021/ma800790w

https://hdl.handle.net/11094/81835