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Creators/Authors contains: "Pochan, Darrin J."

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  1. ; ; ; ; ; ; ; ( , ACS Applied Materials & Interfaces)
    Free, publicly-accessible full text available October 6, 2025
  2. ; ; ; ; ; ; ; ( , Biomacromolecules)
    Free, publicly-accessible full text available June 10, 2025
  3. ; ; ; ( , Bioconjugate Chemistry)
    Full Text Available 
  4. ; ; ; ; ; ; ; ; ; ; et al ( , Biomacromolecules)
  5. ; ; ; ; ; ; ; ; ; ; et al ( , Journal of the American Chemical Society)
    Full Text Available 
  6. ; ; ; ; ; ( , Macromolecules)
    null (Ed.)
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  7. ; ; ; ; ; ; ; ; ; ; et al ( , Journal of the American Chemical Society)
    null (Ed.)
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  8. ; ; ; ; ; ; ( , Angewandte Chemie)
    Abstract

    Thermoresponsive resilin‐like polypeptides (RLPs) of various lengths were genetically fused to two different computationally designed coiled coil‐forming peptides with distinct thermal stability, to develop new strategies to assemble coiled coil peptides via temperature‐triggered phase separation of the RLP units. Their successful production in bacterial expression hosts was verified via gel electrophoresis, mass spectrometry, and amino acid analysis. Circular dichroism (CD) spectroscopy, ultraviolet‐visible (UV/Vis) turbidimetry, and dynamic light scattering (DLS) measurements confirmed the stability of the coiled coils and showed that the thermosensitive phase behavior of the RLPs was preserved in the genetically fused hybrid polypeptides. Cryogenic‐transmission electron microscopy and coarse‐grained modeling revealed that functionalizing the coiled coils with thermoresponsive RLPs leads to their thermally triggered noncovalent assembly into nanofibrillar assemblies.

     
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  9. ; ; ; ; ; ; ( , Angewandte Chemie International Edition)
    Abstract

    Thermoresponsive resilin‐like polypeptides (RLPs) of various lengths were genetically fused to two different computationally designed coiled coil‐forming peptides with distinct thermal stability, to develop new strategies to assemble coiled coil peptides via temperature‐triggered phase separation of the RLP units. Their successful production in bacterial expression hosts was verified via gel electrophoresis, mass spectrometry, and amino acid analysis. Circular dichroism (CD) spectroscopy, ultraviolet‐visible (UV/Vis) turbidimetry, and dynamic light scattering (DLS) measurements confirmed the stability of the coiled coils and showed that the thermosensitive phase behavior of the RLPs was preserved in the genetically fused hybrid polypeptides. Cryogenic‐transmission electron microscopy and coarse‐grained modeling revealed that functionalizing the coiled coils with thermoresponsive RLPs leads to their thermally triggered noncovalent assembly into nanofibrillar assemblies.

     
    more » « less
  10. ; ; ; ; ; ; ( , Journal of the American Chemical Society)
    Full Text Available