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Precisely patterned nanofibres made from extendable protein multiplexes.
Bethel, Neville P; Borst, Andrew J; Parmeggiani, Fabio; Bick, Matthew J; Brunette, T J; Nguyen, Hannah; Kang, Alex; Bera, Asim K; Carter, Lauren; Miranda, Marcos C; Kibler, Ryan D; Lamb, Mila; Li, Xinting; Sankaran, Banumathi; Baker, David.
Afiliação
  • Bethel NP; Department of Biochemistry, University of Washington, Seattle, WA, USA.
  • Borst AJ; Institute for Protein Design, University of Washington, Seattle, WA, USA.
  • Parmeggiani F; Howard Hughes Medical Institute, University of Washington, Seattle, WA, USA.
  • Bick MJ; Department of Biochemistry, University of Washington, Seattle, WA, USA.
  • Brunette TJ; Institute for Protein Design, University of Washington, Seattle, WA, USA.
  • Nguyen H; School of Chemistry, University of Bristol, Bristol, UK.
  • Kang A; School of Biochemistry, University of Bristol, Bristol, UK.
  • Bera AK; Bristol Biodesign Institute, University of Bristol, Bristol, UK.
  • Carter L; Department of Biochemistry, University of Washington, Seattle, WA, USA.
  • Miranda MC; Institute for Protein Design, University of Washington, Seattle, WA, USA.
  • Kibler RD; Department of Biochemistry, University of Washington, Seattle, WA, USA.
  • Lamb M; Institute for Protein Design, University of Washington, Seattle, WA, USA.
  • Li X; Department of Biochemistry, University of Washington, Seattle, WA, USA.
  • Sankaran B; Institute for Protein Design, University of Washington, Seattle, WA, USA.
  • Baker D; Department of Biochemistry, University of Washington, Seattle, WA, USA.
Nat Chem ; 15(12): 1664-1671, 2023 Dec.
Article em En | MEDLINE | ID: mdl-37667012
ABSTRACT
Molecular systems with coincident cyclic and superhelical symmetry axes have considerable advantages for materials design as they can be readily lengthened or shortened by changing the length of the constituent monomers. Among proteins, alpha-helical coiled coils have such symmetric, extendable architectures, but are limited by the relatively fixed geometry and flexibility of the helical protomers. Here we describe a systematic approach to generating modular and rigid repeat protein oligomers with coincident C2 to C8 and superhelical symmetry axes that can be readily extended by repeat propagation. From these building blocks, we demonstrate that a wide range of unbounded fibres can be systematically designed by introducing hydrophilic surface patches that force staggering of the monomers; the geometry of such fibres can be precisely tuned by varying the number of repeat units in the monomer and the placement of the hydrophilic patches.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Nanofibras Idioma: En Revista: Nat Chem Assunto da revista: QUIMICA Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Nanofibras Idioma: En Revista: Nat Chem Assunto da revista: QUIMICA Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos