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1.
Chemistry ; 27(23): 6904-6910, 2021 Apr 21.
Article in English | MEDLINE | ID: mdl-33560564

ABSTRACT

Monodisperse unilamellar nanotubes (NTs) and nanoribbons (NRs) were transformed to multilamellar NRs and NTs in a well-defined fashion. This was done by using a step-wise approach in which self-assembled cationic amino acid amphiphile (AAA) formed the initial NTs or NRs, and added polyanion produced an intermediate coating. Successive addition of cationic AAA formed a covering AAA layer, and by repeating this layer-by-layer (LBL) procedure, multi-walled nanotubes (mwNTs) and nanoribbons were formed. This process was structurally investigated by combining small-angle neutron scattering (SANS) and cryogenic-transmission electron microscopy (cryo-TEM), confirming the multilamellar structure and the precise layer spacing. In this way the controlled formation of multi-walled suprastructures was demonstrated in a simple and reproducible fashion, which allowed to control the charge on the surface of these 1D aggregates. This pathway to 1D colloidal materials is interesting for applications in life science and creating well-defined building blocks in nanotechnology.


Subject(s)
Nanotubes, Carbon , Amino Acids , Microscopy, Electron, Transmission , Nanotechnology , Scattering, Small Angle
2.
Cell Rep ; 13(11): 2597-2609, 2015 Dec 22.
Article in English | MEDLINE | ID: mdl-26686642

ABSTRACT

F-BAR domain proteins regulate and sense membrane curvature by interacting with negatively charged phospholipids and assembling into higher-order scaffolds. However, regulatory mechanisms controlling these interactions are poorly understood. Here, we show that Drosophila Nervous Wreck (Nwk) is autoregulated by a C-terminal SH3 domain module that interacts directly with its F-BAR domain. Surprisingly, this autoregulation does not mediate a simple "on-off" switch for membrane remodeling. Instead, the isolated Nwk F-BAR domain efficiently assembles into higher-order structures and deforms membranes only within a limited range of negative membrane charge, and autoregulation elevates this range. Thus, autoregulation could either reduce membrane binding or promote higher-order assembly, depending on local cellular membrane composition. Our findings uncover an unexpected mechanism by which lipid composition directs membrane remodeling.


Subject(s)
Carrier Proteins/metabolism , Cell Membrane/metabolism , Drosophila Proteins/metabolism , Animals , Carrier Proteins/chemistry , Dimerization , Drosophila/growth & development , Drosophila/metabolism , Drosophila Proteins/chemistry , Larva/metabolism , Liposomes/metabolism , Microscopy, Confocal , Phospholipids/metabolism , Protein Binding , Protein Structure, Tertiary , Static Electricity , src Homology Domains
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