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Item type:Publication, Access status: with files , Hybrid biological hydrogel provides favorable bioenergetic, adhesive, and antioxidative effects on wound healing(American Chemical Society (ACS), 2025-05-18); ; Wound healing is a dynamic and complex process that demands substantial energy expenditure and a biomimetic microenvironment. Developing a simple and effective biological hydrogel to enhance mitochondrial energy metabolism could effectively promote wound healing. To this end, we developed a hybrid biological hydrogel based on Escherichia coli lipoate protein ligase A (LplA), which combines its catalytic and self-assembling properties to promote wound healing. In murine fibroblast L929 cell models, LplA significantly enhances cellular activity and intracellular metabolism, promoting cell proliferation and energy supply. However, cells aggregated into spherical clusters on the pure LplA hydrogel. To address this issue, we integrated glutaraldehyde (GA) as a cross-linker into the LplA hydrogel. The GA-LplA hydrogel enhances cell adhesion and proliferation and, unexpectedly, exhibits higher catalytic activity compared with the pure LplA hydrogel. Furthermore, LplA was observed to decompose H2O2, and the GA-LplA hybrid hydrogel significantly reduced reactive oxygen species (ROS) production. The promise of this hybrid hydrogel is successfully demonstrated in a male mice full-thickness skin defect model with accelerated re-epithelialization and cell proliferation while reducing inflammation.Publicationtype: Journal Article17 11 - Some of the metrics are blocked by yourconsent settings
Item type:Publication, Access status: with files , Quantitative study of H protein lipoylation of the glycine cleavage system and a strategy to increase its activity by co-expression of LplAGlycine cleavage system (GCS) plays a key role in one-carbon (C1) metabolism related to the biosynthesis of a number of key intermediates with significance in both biomedicine and biotechnology. Despite extensive studies of the proteins (H, T, P and L) involved and the reaction mechanisms of this important enzyme complex little quantitative data are available. In this work, we have developed a simple HPLC method for direct analysis and quantification of the apo- and lipoylated forms (H apo and H lip ) of the shuttle protein H, the latter (H lip ) is essential for the function of H protein and determines the activity of GCS. Effects of temperature, concentrations of lipoic acid and H apo and the expression of H protein on its lipoylation were studied. It is found that H lip is as low as only 20-30% of the total H protein with lipoic acid concentration in the range of 10-20 μM and at a favorable temperature of 30 °C. Furthermore, H apo seems to inhibit the overall activity of GCS. We proposed a strategy of co-expressing LplA to improve the lipoylation of H protein and GCS activity. With this strategy the fraction of H lip was increased, for example, from 30 to 90% at a lipoic acid concentration of 20 μM and GCS activity was increased by more than 2.5 fold. This work lays a quantitative foundation for better understanding and reengineering the GCS system.Publicationtype: Journal ArticleScopus© Citations 15 274 234