Homochiral metal–organic framework (MOF) membranes have been recently reported for chiral separations. However, only a few high‐quality homochiral polycrystalline MOF membranes have been fabricated due to the difficulty in crystallization of a chiral MOF layer without defects on porous substrates. Alternatively, mixed matrix membranes (MMMs), which combine potential advantages of MOFs and polymers, have been widely demonstrated for gas separation and water purification. Here we report novel homochiral MOF–polymer MMMs for efficient chiral separation. Homochirality was successfully incorporated into achiral MIL‐53‐NH2 nanocrystals by post‐synthetic modification with amino acids, such as l‐histidine (l‐His) and l‐glutamic acid (l‐Glu). The MIL‐53‐NH‐l‐His and MIL‐53‐NH‐l‐Glu nanocrystals were then embedded into polyethersulfone (PES) matrix to form homochiral MMMs, which exhibited excellent enantioselectivity for racemic 1‐phenylethanol with the highest enantiomeric excess value up to 100 %. This work, as an example, demonstrates the feasibility of fabricating diverse large‐scale homochiral MOF‐based MMMs for chiral separation.

The rugged folding landscapes of functional proteins puts them at risk of misfolding and aggregation. Serine protease inhibitors, or serpins, are paradigms for this delicate balance between function and misfolding. Serpins exist in a metastable state that undergoes a major conformational change in order to inhibit proteases. However, conformational labiality of the native serpin fold renders them susceptible to misfolding, which underlies misfolding diseases such as α1-antitrypsin deficiency. To investigate how serpins balance function and folding, we used consensus design to create conserpin, a synthetic serpin that folds reversibly, is functional, thermostable, and polymerization resistant. Characterization of its structure, folding and dynamics suggest that consensus design has remodeled the folding landscape to reconcile competing requirements for stability and function. This approach may offer general benefits for engineering functional proteins that have risky folding landscapes, including the removal of aggregation-prone intermediates, and modifying scaffolds for use as protein therapeutics.

Background: GAPDH is a glycolytic enzyme that aggregates during disease. Cysteine oxidation is the putative cause of aggregation. Whether GAPDH aggregation influences disease is unknown. Results: Mutating Met-46 renders GAPDH resistant to free radical-induced aggregation. Conclusion: Methionine oxidation, rather than cysteine oxidation, is a primary event that instigates GAPDH aggregation. Significance: Mutating Met-46 in vivo should elucidate whether GAPDH aggregation causally contributes to disease.