Tuneable Fmoc-Phe-(4-X)-Phe-NH₂ nanostructures by variable electronic substitution
Supramolecular structures were produced by in situ enzymatic condensation of Fmoc-Phe-(4-X), where X denotes electron withdrawing or donating groups, with Phe-NH2. The relative contribution of π-stacking and H-bonding interactions can be regulated by the nature of X, resulting in tuneable nanoscale...
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| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2014-01, Vol.50 (73), p.10630-10633 |
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| container_end_page | 10633 |
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| container_issue | 73 |
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| container_title | Chemical communications (Cambridge, England) |
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| creator | Pappas, Charalampos G Abul-Haija, Yousef M Flack, Angela Frederix, Pim W J M Ulijn, Rein V |
| description | Supramolecular structures were produced by in situ enzymatic condensation of Fmoc-Phe-(4-X), where X denotes electron withdrawing or donating groups, with Phe-NH2. The relative contribution of π-stacking and H-bonding interactions can be regulated by the nature of X, resulting in tuneable nanoscale morphologies. |
| doi_str_mv | 10.1039/c4cc04926h |
| format | Article |
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| fulltext | fulltext |
| identifier | ISSN: 1359-7345 |
| ispartof | Chemical communications (Cambridge, England), 2014-01, Vol.50 (73), p.10630-10633 |
| issn | 1359-7345 1364-548X |
| language | eng |
| recordid | cdi_crossref_primary_10_1039_C4CC04926H |
| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Biocatalysis Dipeptides - chemistry Dipeptides - metabolism Hydrogen Bonding Microscopy, Electron, Transmission Nanostructures - chemistry Phenylalanine - chemistry Thermodynamics Thermolysin - chemistry Thermolysin - metabolism |
| title | Tuneable Fmoc-Phe-(4-X)-Phe-NH₂ nanostructures by variable electronic substitution |
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