2016年
Structure-property relationships of photoresponsive inhibitors of the kinesin motor
ORGANIC & BIOMOLECULAR CHEMISTRY
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- 巻
- 14
- 号
- 30
- 開始ページ
- 7202
- 終了ページ
- 7210
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1039/c6ob00951d
- 出版者・発行元
- ROYAL SOC CHEMISTRY
Recently we demonstrated the photoregulation of the activity of kinesin-1 using an azobenzene-tethered peptide (azo-peptide: Azo-Ile-Pro-Lys-Ala-Ile-Gln-Ala-Ser-His-Gly-Arg-OH). To understand the mechanism behind this photoswitchable inhibition, here we studied the structure-property relationships of a range of azo-peptides through systematic variations in the structures of the peptide and azobenzene units. The vital peptide sequence for kinesin inhibition-mediated through electrostatic, hydrophobic and C-H center dot center dot center dot pi interactions-was the same as that for the self-inhibition of kinesin. We also identified substituents on the azobenzene capable of enhancing the photoswitchability of inhibition. As a result, we developed a new inhibitor featuring a relatively short peptide unit (-Arg-Ile-Pro-Lys-Ala-Ile-Arg-OH) and an azobenzene unit bearing a para-OMe group. In the trans form of its azobenzene unit, this finely tuned inhibitor stopped the kinesin-driven gliding motility of microtubules completely at a relatively low concentration, yet allowed gliding motility with a relatively high velocity in the cis form obtained after UV irradiation.
- リンク情報
- ID情報
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- DOI : 10.1039/c6ob00951d
- ISSN : 1477-0520
- eISSN : 1477-0539
- PubMed ID : 27270305
- Web of Science ID : WOS:000381418900008