COACERVATION AND CALCIUM ION BINDING PROPERTIES OF ELASTIN-DERIVED POLYPEPTIDE, (VAL-PRO-GLY-VAL-GLY)

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概要

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• Elastin is the major component of elastic fibers in connective tissues such as arterial walls, ligaments, lungs and skin, and imparts elasticity to these tissues. The self-association of tropoelastin. a precursor of elastin, is the most significant step in the process of elastin biosynthesis and is called coacervation. The most prominent common repeats in human, bovine, porcine and chick tropoelastin molecules is the pentapeptide sequence (Val-Pro-Gly-Val-Gly, VPGVG). This polypeptide (VPGVG)n is known tocoacervate similarly as tropoelastin. To investigate the contribution of each amino acid residue in (VPGVG)n to coacervation, polypeptide (VPGVG)n and its three analogues, (VPGV)n where G at position 5 is eliminated, (VPG)n where V and G at position 4 and 5 are eliminated, and (PGVG)n where V at position 1 is eliminated, were synthesized and examined by turbidity measurement at 400 nm. As a result, only (VPGVG)n exhibited completely reversible coacervation. Furthermore. the secondary structures of these polypeptides associated with coacervation were discussed by CD and ET-IR studies. It is well known that accumulation of calcium salts on elastin fibers is related to diseases of arterial walls. The interaction of elastin-derived peptides with calcium and other metal ions were examined. In the CD spectra of α-elastin and (VPGVG)n in the presence of metal ions. Ca^<2+> ion induced conformational changes from β-turn to less ordered conformation. Although this conformational change is also caused by Mg^<2+> ion, it was a smaller change compared to Ca^<2+> effect. On the other hand, it is shown that Na^+ ion had little effect. The ^<13>C-NMR spectra were measured using the carbonyl region of ^<13>C-enriched (VPGVG)n in the presence of metal ions. There were large changes in chemical shifts of Gly^3C-O, Val^4C-O and Gly^5C-O resonances on addition of Ca^<2+> ion. Furthermore, broad resonances in the presence of Ca^<2+> ion were observed. These results suggest that Ca^<2+> ion induces the conformational change of (VPGVG)n by binding to peptide carbonyls of Gly^3, Val^4, and Gly^5 residues.

• 日本結合組織学会の論文

著者

• 岡本 研

  日本医科大学大学院医科生物化学分野

• 岡本 研

  日本医科大学生化学分子生物学講座(構造生物学・代謝学)

• MAEDA Iori

  Department of Chemistry, Faculty of Science, Kyushu University

• Maeda I

  Department Of Bioscience And Bioinformatics Kyushu Institute Of Technology

• Maeda Iori

  Department Of Biochemical Engineering And Science Kyushu Institute Of Technology

• UEMURA Yuko

  Department of Biochemical Engineering and Science, Kyushu Institute of Technology

• OKAMOTO Kouji

  Department of Biochemical Engineering and Science, Kyushu Institute of Technology

• Okamoto K

  Department Of Bioscience And Bioinformatics Kyushu Institute Of Technology

• Okamoto Kouji

  Department Of Biochemical Engineering And Science Kyushu Institute Of Technology

• FUKUMOTO Yoshiteru

  Department of Bioscience and Bioinformatics, Kyushu Institute of Technology

• Uemura Yuko

  Department Of Biochemical Engineering And Science Kyushu Institute Of Technology

• Kondo M

  Department Of Health And Welfare Nishikyushu University

• Kaibara K

  Department Of Biological Substances And Life Science Faculty Of Engineering Kyushu Kyoritsu Universi

• Kaibara Kozue

  Department Of Biological Substances And Life Science Faculty Of Engineering Kyushu Kyoritsu Universi

• KONDO Michio

  Faculty of Sicence and Engineering, Saga University

• Kaibara Kozue

  Graduate School of Science, Kyushu University

• Kondo Michio

  Faculty Of Science And Engineering Saga University

• Okamoto Kouji

  Department Of Biochemical Engineering And Science Kyusyu Institute Of Technology

• Fukumoto Yoshiteru

  Department Of Bioscience And Bioinformatics Kyushu Institute Of Technology

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