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 inAngewandte Chemie International Edition Vol. 50; no. 16; pp. 3715 - 3719
Main Authors Ke, Damei, Zhan, Chuanlang, Li, Alexander D. Q., Yao, Jiannian
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 11.04.2011
WILEY‐VCH Verlag
Wiley
Wiley Subscription Services, Inc
EditionInternational ed. in English
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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.
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).
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ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201006897