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Homochiral nanochannel membrane separated amino acid enantiomers

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Research area:engineering-energy

What the study found

The study found that a homochiral hydrogen-bonded biohybrid framework built inside poly(ethylene terephthalate) nanochannels enabled highly selective separation of amino acid enantiomers. It achieved near-complete resolution of racemic histidine, with d-histidine transported preferentially.

Why the authors say this matters

The authors conclude that this work offers a scalable platform for high-efficiency chiral separations, especially for pharmaceutical applications. They also present it as a way to address the challenge of combining strong enantioselectivity with robust flux in nanochannel membranes.

What the researchers tested

The researchers used a voltage-driven in situ assembly strategy to construct a homochiral hydrogen-bonded biohybrid framework, called HBF, within poly(ethylene terephthalate) nanochannels, forming HBF@PET membranes. The framework was built using directional hydrogen bonding between bovine serum albumin, a protein, and 1,3,6,8-tetra(terephthalic acid) pyrene.

What worked and what didn't

The HBF@PET membrane separated racemic histidine with enantiomeric excess above 99% and a d-histidine flux of 4.52 ± 0.04 mmol m–2 h–1, which the abstract says surpasses state-of-the-art nanochannel systems. Mechanistic studies indicated stronger binding of the framework to l-histidine, which hindered its diffusion while helping d-histidine pass more readily; the membrane also showed applicability to tryptophan and arginine enantiomers.

What to keep in mind

The limitations described in the available abstract are limited. The report states that the membrane was tested for histidine and also for tryptophan and arginine enantiomers, but it does not provide broader performance limits, long-term durability data, or details beyond the summary provided.

Key points

  • A homochiral hydrogen-bonded biohybrid framework was assembled inside PET nanochannels.
  • The membrane resolved racemic histidine with enantiomeric excess above 99%.
  • d-Histidine was transported at 4.52 ± 0.04 mmol m–2 h–1.
  • Mechanistic studies found stronger binding to l-histidine than to d-histidine.
  • The membrane also showed applicability to tryptophan and arginine enantiomers.

Disclosure

Research title:
Homochiral nanochannel membrane separated amino acid enantiomers
Authors:
Xinyue Chang, Yanxia Song, Liping Zhen, Ningshuang Gao, Zhiwen Zhao, Genping Meng, JINGLAI DUAN, Baodui Wang
Institutions:
Chinese Academy of Sciences, Institute of Modern Physics, Ji Hua Laboratory, Ji Hua Laboratory, Lanzhou University, Lanzhou University, Lanzhou University, Lanzhou University, Lanzhou University, Lanzhou University, Lanzhou University, PRG S&Tech (South Korea), PRG S&Tech (South Korea), State Key Laboratory of Chemical Engineering, State Key Laboratory of Chemical Engineering, State Key Laboratory of Chemical Engineering, State Key Laboratory of Chemical Engineering, State Key Laboratory of Chemical Engineering, State Key Laboratory of Chemical Engineering, State Key Laboratory of Chemical Engineering, University of Science and Technology of China
Publication date:
2026-02-24
DOI:
10.1021/jacs.5c22150
OpenAlex record:
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AI provenance: This post was generated by gpt-5.4-mini (OpenAI). The original authors did not write or review this post.

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