Role of His16 in the structural flexibility of the C-terminal region of human endothelin-1

Hirotsugu Hiramatsu, Hiroki Aduma, Yuriko Tanaka, Takashi Miura, Hideo Takeuchi

研究成果: Article査読

1 被引用数 (Scopus)

抄録

The biological activity of endothelin-1 (ET-1), a 21-residue vasoconstrictive peptide hormone, has been reported to largely increase upon substitution of Ala for His16. We have investigated possible differences in structural properties between wild type ET-1 and its H16A mutant by using circular dichroism, ultraviolet resonance Raman, visible Raman, and infrared absorption spectroscopy. The C-terminal region of ET-1 spanning from His16 to Trp21 is found to be sensitive to the environment and folds into an α-helical structure under hydrophobic conditions. The environmental sensitivity is elevated in the H16A mutant. A pH decrease from 7.0 to 5.5 does not affect the secondary structure of WT ET-1 but induces an α-helical structure in the H16A mutant. These observations indicate that the mutation of His16 to Ala significantly increases the flexibility of the C-terminal region. The increased flexibility of the H16A mutant may be advantageous for efficient but not for specific binding to receptors. His16 may play an important role in maintaining the structural flexibility of the C-terminal region at an appropriate level and keeping a high specificity to the endothelin receptors.

本文言語English
ページ(範囲)328-332
ページ数5
ジャーナルJournal of Molecular Structure
976
1-3
DOI
出版ステータスPublished - 2010 7 15

ASJC Scopus subject areas

  • 分析化学
  • 分光学
  • 有機化学
  • 無機化学

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