Premium
Ultrathin Polydopamine Films with Phospholipid Nanodiscs Containing a Glycophorin A Domain
Author(s) -
Marchesi D'Alvise Tommaso,
Harvey Sean,
Hueske Lisa,
Szelwicka Jolanta,
Veith Lothar,
Knowles Tuomas P. J.,
Kubiczek Dennis,
Flaig Carolin,
Port Fabian,
Gottschalk KayE.,
Rosenau Frank,
Graczykowski Bartlomiej,
Fytas George,
Ruggeri Francesco S.,
Wunderlich Katrin,
Weil Tanja
Publication year - 2020
Publication title -
advanced functional materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.069
H-Index - 322
eISSN - 1616-3028
pISSN - 1616-301X
DOI - 10.1002/adfm.202000378
Subject(s) - materials science , membrane , nanopore , nanodisc , nanotechnology , glycophorin , dispersity , lipid bilayer , biophysics , polymer chemistry , chemistry , biochemistry , biology
Abstract Cellular membranes have long served as an inspiration for nanomaterial research. The preparation of ultrathin polydopamine (PDA) films with integrated protein pores containing phospholipids and an embedded domain of a membrane protein glycophorin A as simplified cell membrane mimics is reported. Large area, ultrathin PDA films are obtained by electropolymerization on gold surfaces with 10–18 nm thickness and dimensions of up to 2.5 cm 2 . The films are transferred from gold to various other substrates such as nylon mesh, silicon, or substrates containing holes in the micrometer range, and they remain intact even after transfer. The novel transfer technique gives access to freestanding PDA films that remain stable even at the air interfaces with elastic moduli of ≈6–12 GPa, which are higher than any other PDA films reported before. As the PDA film thickness is within the range of cellular membranes, monodisperse protein nanopores, so‐called “nanodiscs,” are integrated as functional entities. These nanodisc‐containing PDA films can serve as semi‐permeable films, in which the embedded pores control material transport. In the future, these simplified cell membrane mimics may offer structural investigations of the embedded membrane proteins to receive an improved understanding of protein‐mediated transport processes in cellular membranes.