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- W2127137760 endingPage "4245" @default.
- W2127137760 startingPage "4238" @default.
- W2127137760 abstract "Abstract The self‐assembly of molecules into desired architectures is currently a challenging subject for the development of supramolecular chemistry. Here we present a facile “breath figure” assembly process through the use of the self‐assembled peptide building block diphenylalanine ( L ‐Phe‐ L ‐Phe, FF). Macroporous honeycomb scaffolds were fabricated, and average pore size could be regulated, from (1.00±0.18) μm to (2.12±0.47) μm, through the use of different air speeds. It is indicated that the honeycomb formation is humidity‐, solvent‐, concentration‐, and substrate‐dependent. Moreover, water molecules introduced from “breath figure” intervene in the formation of hydrogen bonds during FF molecular self‐assembly, which results in a hydrogen bond configuration transition from antiparallel β sheet to parallel β sheet. Meanwhile, as a result of the higher polarity of water molecules, the FF molecular array is transformed from laminar stacking into a hexagonal structure. These findings not only elucidate the FF molecule self‐assembly process, but also strongly support the mechanism of breath figure array formation. Finally, human embryo skin fibroblast (ESF) culture experiments suggest that FF honeycomb scaffolds are an attractive biomaterial for growth of adherent cells with great potential applications in tissue engineering." @default.
- W2127137760 created "2016-06-24" @default.
- W2127137760 creator A5017432130 @default.
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- W2127137760 creator A5063142554 @default.
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- W2127137760 date "2011-03-08" @default.
- W2127137760 modified "2023-10-18" @default.
- W2127137760 title "Honeycomb Self-Assembled Peptide Scaffolds by the Breath Figure Method" @default.
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- W2127137760 doi "https://doi.org/10.1002/chem.201003021" @default.
- W2127137760 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21387428" @default.
- W2127137760 hasPublicationYear "2011" @default.
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