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ST Huber, D Terwiel, WH Evers, D Maresca, AJ Jakobi. Preprint 2022 doi: 10.1101/2022.05.08.489936
Many kinds of bacteria and archaea control their buoyancy to move to optimal positions in liquid environments. They do this by making nano-compartments called "gas vesicles", long "pipes" with closed ends filled with gases. In 2022, gas vesicle structure was solved, revealing self-assembling thin-walled cylinders of remarkable strength with gas-permeable pores and water-repelling (hydrophobic) interiors. Building on this structural knowledge, gas vesicles are being engineered to serve as biosensors that report via ultrasound.

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IB Tomasic, MC Metcalf, AI Guce, NE Clark, SC Garman. J. Biol. Chem. 2010 doi: 10.1074/jbc.M110.118588
The human lysosomal enzymes α-galactosidase and α-N-acetylgalactosaminidase share 46% amino acid sequence identity and have similar folds. Using a rational protein engineering approach, we interconverted the enzymatic specificity of α-GAL and α-NAGAL. The engineered α-GAL retains the antigenicity but has acquired the enzymatic specificity of α-NAGAL. Conversely, the engineered α-NAGAL retains the antigenicity but has acquired the enzymatic specificity of the α-GAL enzyme. Comparison of the crystal structures of the designed enzyme to the wild-type enzymes shows that active sites superimpose well, indicating success of the rational design. The designed enzymes might be useful as non-immunogenic alternatives in enzyme replacement therapy for treatment of lysosomal storage disorders such as Fabry disease.

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Above is a transmembrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (shown above) opens and binds peptide or drug, then closes, while its cytoplasmic face (opposite end from the above) opens to release its cargo into the intestinal cell, which passes it on into the blood circulation.

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