Evidence map›Paper›PMID 40841799›Full record

ArticleNature communications2025

A homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acids.

Ting Xu, Li Cao, Shuhao An, Xiaowei Liu, Zhen Li, Zhiping Lai

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Ting XuCenter of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST), Thuwal, Kingdom of Saudi Arabia.
Li CaoCenter of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST), Thuwal, Kingdom of Saudi Arabia. li.cao@kaust.edu.sa.ORCID http://orcid.org/0000-0002-7087-9431
Shuhao AnCenter of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST), Thuwal, Kingdom of Saudi Arabia.ORCID http://orcid.org/0000-0001-9099-3314
Xiaowei LiuCenter of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST), Thuwal, Kingdom of Saudi Arabia.ORCID http://orcid.org/0000-0002-2577-0701
Zhen LiCenter of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST), Thuwal, Kingdom of Saudi Arabia.ORCID http://orcid.org/0000-0002-7048-9011
Zhiping LaiCenter of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST), Thuwal, Kingdom of Saudi Arabia. zhiping.lai@kaust.edu.sa.ORCID http://orcid.org/0000-0001-9555-6009

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The separation of amino acids from complex mixtures remains an essential yet multi-step, energy-intensive process. Membrane separation technology offers a more energy-efficient alternative, but its effectiveness relies on achieving highly precise molecular recognition. Here, we report a homochiral covalent organic framework (COF) membrane with ordered ultra-microporous pore structures for targeted extraction of specific enantiomer from amino acid mixtures. Benefiting from its high crystallinity and ultra-microporous chiral channels, the membrane exhibits both excellent permeability and enantioselectivity. A combination of experimental results, density functional theory calculations, and molecular dynamics simulations reveal a retarded transport mechanism, wherein stronger interactions between L-enantiomers and the homochiral pores hinder their transmembrane diffusion. We further demonstrate a two-stage cascade membrane process to simultaneously fractionate and enantioseparate amino acid mixtures, achieving near pure (99.5%) D-threonine from an eight-component protein hydrolysis complex. This study offers a promising and sustainable membrane-based solution for efficient amino acid purification.

Indexed as

Amino AcidsChemical FractionationMembranes, ArtificialMetal-Organic FrameworksMolecular Dynamics SimulationPorosityStereoisomerismAmino AcidsMembranes, ArtificialMetal-Organic Frameworks

Identifiers

PMID40841799
PMCPMC12370987

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.