Synthesis of (Pro-Hyp-Gly) n of defined molecular weights. Evidence for the stabilization of collagen triple helix by hydroxypyroline
| Autor: | Shumpei Sakakibara, Katsuhiko Inouye, Darwin J. Prockop, Yasuo Kishida, Yuji Kobayashi, Keiko Shudo |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
animal structures
Time Factors Optical Rotation Proline Stereochemistry Macromolecular Substances Protein Conformation Collagen helix Glycine Cleavage (embryo) Biochemistry Genetics and Molecular Biology (miscellaneous) Merrifield resin Hydroxyproline chemistry.chemical_compound Protein structure Drug Stability Centrifugation Density Gradient Chromatography integumentary system Molecular mass Temperature Molecular Weight chemistry Chromatography Gel Collagen Peptides Oligopeptides |
| Zdroj: | Biochimica et biophysica acta. 303(1) |
| ISSN: | 0006-3002 |
| Popis: | (Pro-Hyp-Gly)5 and (Pro-Hyp-Gly)10 were synthesized by repeated condensation of tert-butyloxycarbonyl(Boc)-Pro-Hyp[benzyl(Bzl)]-Gly on a Merrifield resin followed by cleavage of the peptides from the resin with HF. The solution properties of the peptides were then compared with those of (Pro-Pro-Gly)5 and (Pro-Pro-Gly)10 synthesized previously. The peptides containing hydroxyproline were similar to those that did not, in that they formed triple-helical structures analogous to the triple-helical structure of collagen. At low temperatures the peptides showed a high degree of negative optical rotation and there was a relatively sharp change in optical rotation as the temperature was increased. The T m was about 5 °C for (Pro-Hyp-Gly)5 and about 58 °C for (Pro-Hyp-Gly)10. Ultracentrifugation studies were consistent with the conclusion that the temperature-dependent changes in optical rotation reflected a transition between triple-stranded and single-stranded forms of the peptides. The major difference between the peptides containing hydroxyproline and those that did not was that the T m values for the hydroxyproline-containing peptides were higher by about 35 °C. The results indicated that the hydroxyprolyl residues preceding glycyl residues in the peptides stabilize the triple-helical structure, and they suggested therefore that hydroxyproline may perform a similar function in collagen. |
| Databáze: | OpenAIRE |
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