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Liposomes, Exosomes, and Virosomes: From Modeling Complex

Membrane Processes to Medical Diagnostics and Drug Delivery

Poster Abstracts

68

49-POS

Board 25

Membrane Nucleoporins Form Porous Proteoliposomes with Nuclear Pore-Like Selectivity

Radhakrishnan Panatala

1,2

, Suncica Vujica

1,2

, Yusuke Sakiyama

1,2

, Roderick Lim

1,2

,

2

Swiss Nanoscience Institute, Basel, Basel-Stadt, Switzerland.

1

Biozentrum, Basel, Basel-Stadt,

Switzerland,

Eukaryotic cells maintain order and function by the selective accumulation of essential

macromolecules in the nucleus. This process is regulated by soluble nuclear transport receptors

(NTRs) that gain exclusive access through 50 nm channels known as nuclear pore complexes

(NPCs). Here, we have engineered nanoporous proteoliposomes that harbor key membrane

proteins of the NPC. Using fluorescence-based translocation assays, we observed that these

proteoliposomes show to discriminate against non-specific macromolecules above a certain size-

threshold whereas specific transport factors are transported across the pores. Imported NTRs are

subsequently entrapped within the proteoliposome lumen using wheat germ agglutinin (WGA), a

known NPC blocking agent. In conjunction, we performed morphological characterization of the

nanopores by high-speed atomic force microscopy (HS-AFM), which revealed that the

permeability barrier, composed of FG-nucleoporins, resembles to that of NPCs from

X. laevis

oocyte nuclei. Eventually, we’d like to apply such a macromolecular logistics system to sort and

encapsulate specific molecular modules from a complex environment leading to the construction

of a molecular factory.