期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 24, 期 39, 页码 9754-9759出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201801315
关键词
host-guest interaction; peptides; pillararene; self-assembly; supramolecular chemistry
资金
- National Natural Science Foundation of China [21572101]
- Alexander von Humboldt Foundation
Small peptides capable of assembling into well-defined nanostructures have attracted extensive attention due to their interesting applications as biomaterials. This work reports the first example of a pillararene functionalized with a guanidiniocarbonyl pyrrole (GCP)-conjugated short peptide segment. The obtained amphiphilic peptide 1 spontaneously self-assembles into a supramolecular-sheet in aqueous solution based on host-guest interaction between pillararene and GCP unit as well as hydrogen-bonding between the peptide strands. Interestingly, peptide 1 at low concentration shows transitions from small particles to pearl necklace assemblies, and finally to branched fibers in a time-dependent process. At higher concentration, it directly assembles into twisted beta-sheet tapes. Notably, without pillararene moiety, the control peptideA forms-helix structure with morphology changing from particles to bamboo-like assemblies depending on concentration, indicating a significant role of the pillararene-GCP host-guest interaction for the secondary structure formation. Moreover, peptide 1 can serve as an efficient gene transfection vector.
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