Self-Assembly of β-Sheets into Nanostructures by Poly(alanine) Segments Incorporated in Multiblock Copolymers Inspired by Spider Silk

Selective replacement of the amorphous peptide domain of a spider silk with poly(ethylene glycol) gave N. clavipes silk-inspired polymers having similar solid-state structures and very good mechanical properties. The tendency of poly(alanine) having appropriate chain length to form β-sheets and the...

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Veröffentlicht in:Journal of the American Chemical Society 2001-06, Vol.123 (22), p.5231-5239
Hauptverfasser: Rathore, Osman, Sogah, Dotsevi Y
Format: Artikel
Sprache:eng
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Zusammenfassung:Selective replacement of the amorphous peptide domain of a spider silk with poly(ethylene glycol) gave N. clavipes silk-inspired polymers having similar solid-state structures and very good mechanical properties. The tendency of poly(alanine) having appropriate chain length to form β-sheets and the facility with which the β-sheets self-assemble have been retained in the polymers. Solid-state 13C NMR, solid-state FTIR, X-ray diffraction, and AFM studies showed that the polymers formed predominantly antiparallel β-sheets that self-assembled into discrete nanostructures. The longer the peptide segment was, the greater was the tendency to self-assemble into antiparallel β-sheet aggregates. AFM revealed that the morphology of the polymers was a microphase-separated architecture that contained irregularly shaped 100−200 nm poly(alanine) nanodomains interspersed within the PEG phase. The results suggest that the poly(alanine) domain influences the solid-state properties of spider silk through β-sheet self-assembly into temporary cross-links. The results further demonstrate that by selectively replacing certain segments of a naturally occurring biopolymer with a judiciously selected nonnative segment while, at the same time, retaining other segments known to be critical for the essential properties of the native biopolymer, a synthetic polymer with similar properties and function can be obtained.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja004030d