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Structure and shape effects of molecular glue on supramolecular tubulin assemblies.
Garzoni, Matteo; Okuro, Kou; Ishii, Noriyuki; Aida, Takuzo; Pavan, Giovanni M.
Afiliación
  • Garzoni M; Department of Innovative Technologies, University of Applied Science of Southern Switzerland , Galleria 2, Manno 6928, Switzerland.
ACS Nano ; 8(1): 904-14, 2014 Jan 28.
Article en En | MEDLINE | ID: mdl-24351029
The possibility to arrange biological molecules into ordered nanostructures is an important issue in nano- and biotechnology. Nature offers a wide range of molecular "bricks" (e.g., proteins, oligonucleotides, etc.) that spontaneously assemble into more complex hierarchical systems with unique functionalities. Such molecular building blocks can be also used for the construction of nanomaterials with peculiar properties (e.g., DNA origami). In some cases, molecular glues able to bind biomolecules and to induce their assembly can be used to control the final structure and properties in a convenient way. Here we provide molecular-level description of how molecular glues designed to stick to the surface of microtubules (MTs) can control and transform the α/ß-tubulin assembly upon temperature decreasing. By means of all-atom molecular dynamics (MD) simulations, we compared the adhesion to the MT surface of three molecular glues bearing the same guanidinium ion surface adhesive groups, but having different architecture, i.e., linear or dendritic backbone. Our evidence demonstrates that the adhesive properties of the different molecular glues are dependent on the shape they assume in solution. In particular, adhesion data from our MD simulations explain how globular- or linear-like molecular glues respectively stabilize MTs or transform them into a well-defined array of α/ß-tubulin rings at 15 °C, where MTs naturally depolymerize. The comprehension of the MT transformation mechanism provides a useful rationale for designing ad hoc molecular glues to obtain ordered protein nanostructures from different biological materials.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tubulina (Proteína) Idioma: En Revista: ACS Nano Año: 2014 Tipo del documento: Article País de afiliación: Suiza Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tubulina (Proteína) Idioma: En Revista: ACS Nano Año: 2014 Tipo del documento: Article País de afiliación: Suiza Pais de publicación: Estados Unidos