Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 17, Issue 15, Pages 4238-4245Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201003021
Keywords
breath figure; peptides; scaffolds; self-assembly; supra-molecular chemistry
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Funding
- National Basic Research Program of China [2009CB930100]
- National Natural Science Foundation of China [NNSFC 20833010]
- Alexander von Humboldt Foundation
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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) mm to (2.12 +/- 0.47) mu m, 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 beta sheet to parallel beta 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.
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