期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 18, 期 32, 页码 9834-9840出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201201431
关键词
biomacromolecular interactions; peptides; photochromism; photoregulation; protein engineering
资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan (MEXT) [471, 23750184]
- Grants-in-Aid for Scientific Research [22350072, 23750184] Funding Source: KAKEN
Diarylethene-bridged peptides were developed to photoregulate biomolecular interactions. The peptides are made up of diarylethene-bridged and DNA-binding regions at their N- and C termini, respectively. The two regions could be independently designed and combined as desired. The a-helicities of the peptides were photoregulated in on/off or off/on manners, and the manner depended on the positions of two ornithine (Orn) residues for cross-linking reaction at the diarylethene-bridged region. In the case of the on/off manner, when the diarylethene structure adopted the open form on the peptides, the peptides folded into stable a-helices. Upon UV irradiation, the diarylethene moiety isomerized to its closed form to destabilize the helical structures. Quartz crystal microbalance (QCM) analysis showed that the open isomer strongly associated with a target DNA, as compared with the closed one. When the closed-form peptide existing in the DNA complex was irradiated with a fluorescent lamp in the middle of the QCM monitoring, the frequency change (?F) was enhanced by the diarylethene photoisomerization.
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