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Nanoassembly of spider silk protein mediated by intrinsically disordered regions.
Li, Jiaxin; Yang, Gabriel Z; Li, Xue; Tan, Hao Lei; Wong, Zhi Wei; Jiang, Shimin; Yang, Daiwen.
Afiliación
  • Li J; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.
  • Yang GZ; Department of Chemistry, University of British Columbia, Vancouver, BC V6T 1Z1, Canada.
  • Li X; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.
  • Tan HL; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.
  • Wong ZW; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.
  • Jiang S; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.
  • Yang D; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore. Electronic address: dbsydw@nus.edu.sg.
Int J Biol Macromol ; 271(Pt 1): 132438, 2024 Jun.
Article en En | MEDLINE | ID: mdl-38761906
ABSTRACT
Spider silk is the self-assembling product of silk proteins each containing multiple repeating units. Each repeating unit is entirely intrinsically disordered or contains a small disordered domain. The role of the disordered domain/unit in conferring silk protein storage and self-assembly is not fully understood yet. Here, we used biophysical and biochemical techniques to investigate the self-assembly of a miniature version of a minor ampullate spidroin (denoted as miniMiSp). miniMiSp consists of two identical intrinsically disordered domains, one folded repetitive domain, and two folded terminal domains. Our data indicated that miniMiSp self-assembles into oligomers and further into liquid droplets. The oligomerization is attributed to the aggregation-prone property of both the disordered domains and the folded repetitive domain. Our results support the model of micellar structure for silk proteins at high protein concentrations. The disordered domain is indispensable for liquid droplet formation via liquid-liquid phase separation, and tyrosine residues located in the disordered domain make dominant contributions to stability of the liquid droplets. As the same tyrosine residues are also critical to fibrillation, the liquid droplets are likely an intermediate state between the solution state and the fiber state. Additionally, the terminal domains contribute to the pH- and salt-dependent self-assembly properties.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arañas / Fibroínas / Proteínas Intrínsecamente Desordenadas Límite: Animals Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article País de afiliación: Singapur Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arañas / Fibroínas / Proteínas Intrínsecamente Desordenadas Límite: Animals Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article País de afiliación: Singapur Pais de publicación: Países Bajos