Toward the development of peptide nanofilaments and nanoropes as smart materials

  • Daniel E. Wagner
    Departments of Biology and Physics, Haverford College, 370 Lancaster Avenue, Haverford, PA 19041
  • Charles L. Phillips
    Departments of Biology and Physics, Haverford College, 370 Lancaster Avenue, Haverford, PA 19041
  • Wasif M. Ali
    Departments of Biology and Physics, Haverford College, 370 Lancaster Avenue, Haverford, PA 19041
  • Grant E. Nybakken
    Departments of Biology and Physics, Haverford College, 370 Lancaster Avenue, Haverford, PA 19041
  • Emily D. Crawford
    Departments of Biology and Physics, Haverford College, 370 Lancaster Avenue, Haverford, PA 19041
  • Alexander D. Schwab
    Departments of Biology and Physics, Haverford College, 370 Lancaster Avenue, Haverford, PA 19041
  • Walter F. Smith
    Departments of Biology and Physics, Haverford College, 370 Lancaster Avenue, Haverford, PA 19041
  • Robert Fairman
    Departments of Biology and Physics, Haverford College, 370 Lancaster Avenue, Haverford, PA 19041

書誌事項

公開日
2005-08-29
DOI
  • 10.1073/pnas.0505871102
公開者
Proceedings of the National Academy of Sciences

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説明

<jats:p>Protein design studies using coiled coils have illustrated the potential of engineering simple peptides to self-associate into polymers and networks. Although basic aspects of self-assembly in protein systems have been demonstrated, it remains a major challenge to create materials whose large-scale structures are well determined from design of local protein–protein interactions. Here, we show the design and characterization of a helical peptide, which uses phased hydrophobic interactions to drive assembly into nanofilaments and fibrils (“nanoropes”). Using the hydrophobic effect to drive self-assembly circumvents problems of uncontrolled self-assembly seen in previous approaches that used electrostatics as a mode for self-assembly. The nanostructures designed here are characterized by biophysical methods including analytical ultracentrifugation, dynamic light scattering, and circular dichroism to measure their solution properties, and atomic force microscopy to study their behavior on surfaces. Additionally, the assembly of such structures can be predictably regulated by using various environmental factors, such as pH, salt, other molecular crowding reagents, and specifically designed “capping” peptides. This ability to regulate self-assembly is a critical feature in creating smart peptide biomaterials.</jats:p>

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