Your browser doesn't support javascript.
loading
Genetic Fusion of Thermoresponsive Polypeptides with UCST-type Behavior Mediates 1D Assembly of Coiled-Coil Bundlemers.
Patkar, Sai S; Tang, Yao; Bisram, Arriana M; Zhang, Tianren; Saven, Jeffery G; Pochan, Darrin J; Kiick, Kristi L.
Afiliación
  • Patkar SS; Department of Materials Science and Engineering, University of Delaware, Newark, DE 19716, USA.
  • Tang Y; Department of Materials Science and Engineering, University of Delaware, Newark, DE 19716, USA.
  • Bisram AM; Department of Materials Science and Engineering, University of Delaware, Newark, DE 19716, USA.
  • Zhang T; Department of Materials Science and Engineering, University of Delaware, Newark, DE 19716, USA.
  • Saven JG; Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
  • Pochan DJ; Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
  • Kiick KL; Department of Materials Science and Engineering, University of Delaware, Newark, DE 19716, USA.
Angew Chem Int Ed Engl ; 62(25): e202301331, 2023 06 19.
Article en En | MEDLINE | ID: mdl-36988077
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.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Fusión Génica Idioma: En Revista: Angew Chem Int Ed Engl Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Fusión Génica Idioma: En Revista: Angew Chem Int Ed Engl Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos