Morphological Transformation between Nanofibers and Vesicles in a Controllable Bipyridine-Tripeptide Self-Assembly
Tuning structures: Stimulus‐responsive peptide self‐assembly requires a balance of conformational change and structural continuity of stable β sheets. In an amphiphilic bipyridine–tripeptide model, temperature, and ultrasound switch a reversible morphological transformation between vesicles and nano...
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Published in | Angewandte Chemie International Edition Vol. 50; no. 16; pp. 3715 - 3719 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Weinheim
WILEY-VCH Verlag
11.04.2011
WILEY‐VCH Verlag Wiley Wiley Subscription Services, Inc |
Edition | International ed. in English |
Subjects | |
Online Access | Get full text |
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Summary: | Tuning structures: Stimulus‐responsive peptide self‐assembly requires a balance of conformational change and structural continuity of stable β sheets. In an amphiphilic bipyridine–tripeptide model, temperature, and ultrasound switch a reversible morphological transformation between vesicles and nanofibers (see picture) through the synergistic effects of terminal β‐sheet‐forming peptides, flexible linkers, and rotatable bipyridine groups. |
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Bibliography: | Chinese Academy of Sciences, 973 Projects - No. 2006CB806200; No. 2007CB936401 istex:59C08BDF8DB88B59B033DA2095F3CABB8126AAA8 This work was financially supported by NSFC (Nos. 20973182, 20872145, and 20733006), the Chinese Academy of Sciences, 973 Projects (2006CB806200 and 2007CB936401), and NSF (CHE-0805547). NSF - No. CHE-0805547 NSFC - No. 20973182; No. 20872145; No. 20733006 ark:/67375/WNG-0DG8RWX3-1 ArticleID:ANIE201006897 This work was financially supported by NSFC (Nos. 20973182, 20872145, and 20733006), the Chinese Academy of Sciences, 973 Projects (2006CB806200 and 2007CB936401), and NSF (CHE‐0805547). ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/anie.201006897 |