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Protein-Eye View of the in Meso Crystallization Mechanism.
van T Hag, Leonie; de Campo, Liliana; Tran, Nhiem; Sokolova, Anna; Trenker, Raphael; Call, Matthew E; Call, Melissa J; Garvey, Christopher J; Leung, Anna E; Darwish, Tamim A; Krause-Heuer, Anwen; Knott, Robert; Meikle, Thomas G; Drummond, Calum J; Mezzenga, Raffaele; Conn, Charlotte E.
Afiliación
  • van T Hag L; Department of Health Sciences and Technology , ETH Zurich , CH-8092 Zurich , Switzerland.
  • Tran N; School of Science, College of Science, Engineering and Health , RMIT University , Melbourne , Victoria 3001 , Australia.
  • Trenker R; Structural Biology Division , The Walter and Eliza Hall Institute of Medical Research , Parkville , Victoria 3052 , Australia.
  • Call ME; Department of Medical Biology , The University of Melbourne , Parkville , Victoria 3052 , Australia.
  • Call MJ; Structural Biology Division , The Walter and Eliza Hall Institute of Medical Research , Parkville , Victoria 3052 , Australia.
  • Garvey CJ; Department of Medical Biology , The University of Melbourne , Parkville , Victoria 3052 , Australia.
  • Leung AE; Structural Biology Division , The Walter and Eliza Hall Institute of Medical Research , Parkville , Victoria 3052 , Australia.
  • Darwish TA; Department of Medical Biology , The University of Melbourne , Parkville , Victoria 3052 , Australia.
  • Knott R; Scientific Activities Division , European Spallation Source ERIC , Lund 224 84 , Sweden.
  • Conn CE; School of Science, College of Science, Engineering and Health , RMIT University , Melbourne , Victoria 3001 , Australia.
Langmuir ; 35(25): 8344-8356, 2019 06 25.
Article en En | MEDLINE | ID: mdl-31122018
For evolving biological and biomedical applications of hybrid protein?lipid materials, understanding the behavior of the protein within the lipid mesophase is crucial. After more than two decades since the invention of the in meso crystallization method, a protein-eye view of its mechanism is still lacking. Numerous structural studies have suggested that integral membrane proteins preferentially partition at localized flat points on the bilayer surface of the cubic phase with crystal growth occurring from a local fluid lamellar L? phase conduit. However, studies to date have, by necessity, focused on structural transitions occurring in the lipid mesophase. Here, we demonstrate using small-angle neutron scattering that the lipid bilayer of monoolein (the most commonly used lipid for in meso crystallization) can be contrast-matched using deuteration, allowing us to isolate scattering from encapsulated peptides during the crystal growth process for the first time. During in meso crystallization, a clear decrease in form factor scattering intensity of the peptides was observed and directly correlated with crystal growth. A transient fluid lamellar L? phase was observed, providing direct evidence for the proposed mechanism for this technique. This suggests that the peptide passes through a transition from the cubic QII phase, via an L? phase to the lamellar crystalline Lc phase with similar layered spacing. When high protein loading was possible, the lamellar crystalline Lc phase of the peptide in the single crystals was observed. These findings show the mechanism of in meso crystallization for the first time from the perspective of integral membrane proteins.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cristalización / Membrana Dobles de Lípidos Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2019 Tipo del documento: Article País de afiliación: Suiza Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cristalización / Membrana Dobles de Lípidos Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2019 Tipo del documento: Article País de afiliación: Suiza Pais de publicación: Estados Unidos