Literature DB >> 26367107

Durable protein lattices of clathrin that can be functionalized with nanoparticles and active biomolecules.

P N Dannhauser1,2, M Platen3, H Böning1, I A T Schaap3,4.   

Abstract

Biological molecules that self-assemble and interact with other molecules are attractive building blocks for engineering biological devices. DNA has been widely used for the creation of nanomaterials, but the use of proteins remains largely unexplored. Here, we show that clathrin can form homogeneous and extended two-dimensional lattices on a variety of substrates, including glass, metal, carbon and plastic. Clathrin is a three-legged protein complex with unique self-assembling properties and is relevant in the formation of membrane transport vesicles in eukaryotic cells. We used a fragment of the adaptor protein epsin to immobilize clathrin lattices on the substrates. The lattices span multiple square millimetres with a regular periodicity of 30 nm and can be functionalized via modified subunits of clathrin with either inorganic nanoparticles or active enzymes. The lattices can be stored for months after crosslinking and stabilization with uranyl acetate. They could be dehydrated and rehydrated without loss of function, offering potential applications in sensing and as biosynthetic reactors.

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Year:  2015        PMID: 26367107     DOI: 10.1038/nnano.2015.206

Source DB:  PubMed          Journal:  Nat Nanotechnol        ISSN: 1748-3387            Impact factor:   39.213


  30 in total

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Journal:  Science       Date:  2005-12-09       Impact factor: 47.728

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Authors:  Paul W K Rothemund
Journal:  Nature       Date:  2006-03-16       Impact factor: 49.962

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Journal:  Chem Commun (Camb)       Date:  2014-01-14       Impact factor: 6.222

Review 4.  Diversity of clathrin function: new tricks for an old protein.

Authors:  Frances M Brodsky
Journal:  Annu Rev Cell Dev Biol       Date:  2012-07-23       Impact factor: 13.827

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Journal:  Cell       Date:  1979-02       Impact factor: 41.582

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Authors:  E Ungewickell; H Ungewickell
Journal:  J Biol Chem       Date:  1991-07-05       Impact factor: 5.157

7.  Conformation switching of clathrin light chain regulates clathrin lattice assembly.

Authors:  Jeremy D Wilbur; Peter K Hwang; Joel A Ybe; Michael Lane; Benjamin D Sellers; Matthew P Jacobson; Robert J Fletterick; Frances M Brodsky
Journal:  Dev Cell       Date:  2010-05-18       Impact factor: 12.270

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Authors:  F K Winkler; K K Stanley
Journal:  EMBO J       Date:  1983       Impact factor: 11.598

9.  Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin.

Authors:  S E Holstein; H Ungewickell; E Ungewickell
Journal:  J Cell Biol       Date:  1996-11       Impact factor: 10.539

10.  An enzyme that removes clathrin coats: purification of an uncoating ATPase.

Authors:  D M Schlossman; S L Schmid; W A Braell; J E Rothman
Journal:  J Cell Biol       Date:  1984-08       Impact factor: 10.539

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  4 in total

1.  Utilizing clathrin triskelions as carriers for spatially controlled multi-protein display.

Authors:  Michael B Deci; Scott W Ferguson; Maixian Liu; Damian C Peterson; Sujatha P Koduvayur; Juliane Nguyen
Journal:  Biomaterials       Date:  2016-08-28       Impact factor: 12.479

2.  Concentration Dependent Ion-Protein Interaction Patterns Underlying Protein Oligomerization Behaviours.

Authors:  Helena Batoulis; Thomas H Schmidt; Pascal Weber; Jan-Gero Schloetel; Christian Kandt; Thorsten Lang
Journal:  Sci Rep       Date:  2016-04-07       Impact factor: 4.379

3.  Dynamical Majorana edge modes in a broad class of topological mechanical systems.

Authors:  Emil Prodan; Kyle Dobiszewski; Alokik Kanwal; John Palmieri; Camelia Prodan
Journal:  Nat Commun       Date:  2017-02-23       Impact factor: 14.919

4.  Zwitterion Effect of Cow Brain Protein towards Efficiency Improvement of Dye-Sensitized Solar Cell (DSSC).

Authors:  Denny Widhiyanuriyawan; Prihanto Trihutomo; Sudjito Soeparman; Lilis Yuliati
Journal:  ScientificWorldJournal       Date:  2020-02-19
  4 in total

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