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      Self-assembly of beta-sheets into nanostructures by poly(alanine) segments incorporated in multiblock copolymers inspired by spider silk.

      Journal of the American Chemical Society
      Amino Acid Sequence, Animals, Calorimetry, Differential Scanning, Microscopy, Atomic Force, Molecular Sequence Data, Peptides, chemistry, Spectroscopy, Fourier Transform Infrared, Spiders, X-Ray Diffraction

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          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 beta-sheets and the facility with which the beta-sheets self-assemble have been retained in the polymers. Solid-state (13)C NMR, solid-state FTIR, X-ray diffraction, and AFM studies showed that the polymers formed predominantly antiparallel beta-sheets that self-assembled into discrete nanostructures. The longer the peptide segment was, the greater was the tendency to self-assemble into antiparallel beta-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 beta-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.

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