Cry3Aa is a protein that forms crystals naturally in the bacterium Bacillus thuringiensis. Here we report that coexpression of Cry3Aa and a Proteus mirabilis lipase without recombinant fusion results in the efficient passive entrapment of the lipase within the nanoporous channels of the resulting crystals. This Cry3Aa crystal-mediated entrapment provides multiple benefits to the lipase including a high enzyme loading, significantly improved thermostability, increased proteolytic resistance, and the ability to be utilized as a recyclable biodiesel catalyst. These characteristics, along with its greatly simplified method of isolation, highlight the potential of Cry3Aa crystal-mediated enzyme entrapment for use in biocatalysis and other biotechnological applications.N anoporous crystalline materials are invaluable frameworks for gas storage, 1,2 molecular separations, 3,4 catalysis, 5−7 and medical applications, 8−10 among others. 11−13 Such materials can be synthesized from metal−organic frameworks, 14,15 activated carbon, 16,17 zeolites, 18 aerogels, 19,20 and even biological components such as DNA 21,22 and proteins. 12,23,24 Each of these systems has its advantages, but the attraction of using protein-based frameworks is their ability to be modified by genetic manipulation with spatial precision, their biodegradability, and their diversity and tunability given the plethora of canonical and noncanonical amino acids 25,26 available.Recently, there has been growing interest in using nanoporous crystalline materials to entrap enzymes for the fabrication of stable and recyclable catalysts. 27−29 In these frameworks it is essential that the scaffold contains nanopores large enough to accommodate protein biomolecules. 30

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The N-terminal domain of Cry3Aa can be used to generate sub-micron particles Genetic fusion of functional peptides to protein particles targets them to A549 cells Myoglobin is an effective oxygen carrier for delivery of O 2 into hypoxic cancer cellsTargeted myoglobin delivery to hypoxic cancer cells increased their radiosensitivity

Follistatin like-1 (Fstl1) is a secreted glycoprotein and can be up-regulated by TGF-β1. To better study the function of Fstl1 in lung development, we examined Fstl1 expression in the developing lung, in a cell type specific manner, using a tamoxifen inducible Fstl1-reporter mouse strain. Our results show that Fstl1 is ubiquitously expressed at saccular stage in the developing lung. At E18.5, Fstl1 expression is robust in most type of mesenchymal cells, including airway smooth muscle cells surrounding airways, vascular smooth muscle cells, endothelial cells, and vascular pericytes from blood vessel, but not PDGFRα fibroblasts in the distal alveolar sacs. Meanwhile, relative weak and sporadic signals of Fstl1 expression are observed in epithelium, including a subgroup of club cells in proximal airways and a few type II alveolar epithelial cells in distal airways. Our data help to understand the critical role of Fstl1 in lung development and lung disease pathogenesis.