An abiotic analogue of the nuclear pore complex hydrogel. Academic Article

abstract

• We describe an abiotic hydrogel that mimics selectivity of the nuclear pore complex. Copolymerization of peptide tetramers (phenylalanine-serine-phenylalanine-glycine, FSFG) with acrylamide results in hydrophobic interactions significant enough to allow the formation of freestanding hydrogel structures. Incorporation of FSFG motifs also renders the hydrogels selective. Selective binding of importins and nuclear transport receptor-cargo complexes is qualitatively demonstrated and compared with polyacrylamide, hydrogels prepared from a control peptide, and hydrogels prepared from the nuclear pore complex protein Nsp1. These abiotic hydrogels will enable further studies of the unique transport mechanisms of the nuclear pore complex and provide an interesting paradigm for the future development of synthetic platforms for separations and selective interfaces.

authors

• Baker, Lane

published proceedings

• Biomacromolecules

author list (cited authors)

• Bird, S. P., & Baker, L. A.

citation count

• 7

complete list of authors

• Bird, Sean P||Baker, Lane A

publication date

• September 2011

publisher

• American Chemical Society (ACS)  Publisher

published in

• Biomacromolecules  Journal

keywords

• Acrylamide
• Acrylic Resins
• Active Transport, Cell Nucleus
• Glycine
• Hydrogels
• Hydrophobic And Hydrophilic Interactions
• Karyopherins
• Microscopy, Fluorescence
• Molecular Mimicry
• Nuclear Pore
• Nuclear Pore Complex Proteins
• Oligopeptides
• Phenylalanine
• Polymerization
• Serine

PubMed Central ID

• 21853987

Digital Object Identifier (DOI)

• 10.1021/bm200820x

start page

• 3119

end page

• 3123

volume

• 12

issue

• 9

URL

• http://dx.doi.org/10.1021/bm200820x