Self-assembled membrane composed of amyloid-like proteins for efficient size-selective molecular separation and dialysis

Facui Yang,Fei Tao,Chen Li,Lingxiang Gao,Peng Yang

doi:10.1038/s41467-018-07888-2

Facui Yang, Fei Tao + Show 3 more

Open Access

https://doi.org/10.1038/s41467-018-07888-2

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Journal: Nature Communications	Publication Date: Dec 1, 2018
Citations: 90	License type: open-access

Affiliation: Shaanxi Normal University

Abstract

The design and scalable construction of robust ultrathin protein membranes with tunable separation properties remain a key challenge in chemistry and materials science. Here, we report a macroscopic ultrathin protein membrane with the potential for scaled-up fabrication and excellent separation efficiency. This membrane, which is formed by fast amyloid-like lysozyme aggregation at air/water interface, has a controllable thickness that can be tuned to 30–250 nm and pores with a mean size that can be tailored from 1.8 to 3.2 nm by the protein concentration. This membrane can retain > 3 nm molecules and particles while permitting the transport of small molecules at a rate that is 1~4 orders of magnitude faster than the rate of existing materials. This membrane further exhibits excellent hemodialysis performance, especially for the removal of middle-molecular-weight uremic toxins, which is 5~6 times higher in the clearance per unit area than the typical literature values reported to date.

Highlights

The design and scalable construction of robust ultrathin protein membranes with tunable separation properties remain a key challenge in chemistry and materials science
We reveal that pores with a mean size that can be tailored from 2 to 3 nm are spontaneously formed by adjacent amyloid-like lysozyme oligomers assembled as a nanomembrane at the air/water interface
The functional groups on the membrane surface were characterized by X-ray Photoelectron Spectroscopy (XPS), which presented the structures on the membrane surface mainly including alphatic carbon (C-H/C-C), amines (C-N), hydroxyls (C-O), thiols (C-S), amides (O=C-N) and carboxyl groups (O=C-O) (Supplementary Fig. 2)

Summary

Introduction

The design and scalable construction of robust ultrathin protein membranes with tunable separation properties remain a key challenge in chemistry and materials science. We report a macroscopic ultrathin protein membrane with the potential for scaled-up fabrication and excellent separation efficiency This membrane, which is formed by fast amyloid-like lysozyme aggregation at air/water interface, has a controllable thickness that can be tuned to 30–250 nm and pores with a mean size that can be tailored from 1.8 to 3.2 nm by the protein concentration. We reveal that pores with a mean size that can be tailored from 2 to 3 nm are spontaneously formed by adjacent amyloid-like lysozyme oligomers assembled as a nanomembrane at the air/water interface This membrane with a controllable nanoscale thickness and large area (e.g., diagonal of 20 in.) readily supports fast dialysis at a transport rate that is 1–4 orders of magnitude faster than the rate of existing materials, allowing the universal and rapid separation of small molecules (e.g., dyes), middle molecules (e.g., toxins) and macromolecules (e.g., proteins) as well as nanoparticles. This membrane exhibits excellent hemodialysis performance, especially for the removal of middle-molecular-weight uremic toxins, while maintaining a nearly 100% retention of serum proteins; this performance is 5–6 times higher in the clearance per unit area than the typical literature values

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