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Photo-responsive systems provide a powerful tool to reversibly regulate enzyme activity. However, inhibitor-based strategies, though widely used, are often restricted to specific enzymes. Noninhibitor strategies, such as enzyme surface modification or genetic mutation, often compromise structural integrity or residual activity. Inspired by the gating mechanisms of biological membranes, we reported a visible light-driven membrane-bound compartment system constructed from phenylazothiazole gated lipids and phospholipids. In this design, phenylazothiazole lipids undergo reversible isomerization between trans and cis configurations under alternating purple and green light, generating continuous nanomechanical motions that transiently enhance membrane permeability. This dynamic gating behavior enables substrate diffusion across the membrane under light exposure and allows the activity of encapsulated enzymes to be switched on and off in a noninvasive, temporally defined manner. This system requires no chemical modification or mutagenesis, thus preserving the native structure and activity of encapsulated enzymes. Beyond binary regulation, precise modulation of the irradiation pattern permits graded control over enzyme activity, offering an advanced level of functional tunability. Using carbonic anhydrase, catalase, and glucose oxidase as models, we demonstrate that enzyme activity can be reversibly and quantitatively regulated via programmable light inputs. This strategy offers a broadly applicable and biocompatible platform for spatiotemporal enzyme regulation.
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http://dx.doi.org/10.1002/anie.202513676 | DOI Listing |
J Agric Food Chem
September 2025
College of Plant Protection, Northwest A&F University, Yangling, Shaanxi 712100, China.
Protoporphyrinogen oxidase (PPO, EC 1.3.3.
View Article and Find Full Text PDFSci Transl Med
September 2025
Burn Injury Research Unit, School of Biomedical Sciences, University of Western Australia, Perth, Western Australia 6009, Australia.
Skin scars remain a substantial clinical challenge because of their impact on appearance and psychological well-being. Lysyl oxidases catalyze collagen cross-linking, a key factor in scar development. Here, we report a randomized, double-blind, placebo-controlled phase 1 study to assess the safety and tolerability of PXS-6302, a topical pan-lysyl oxidase inhibitor, in treating mature scars (ACTRN12621001545853).
View Article and Find Full Text PDFPLoS One
September 2025
Laboratório de Termitologia, Departamento de Sistemática e Ecologia, Centro de Ciências Exatas e da Natureza, Universidade Federal da Paraíba, João Pessoa, Paraíba, Brazil.
With the aim of expanding the possibilities of identifying termite species, in the present study we generated genetic data based on sequences of the mitochondrial gene encoding cytochrome c oxidase subunit II (COII) for termites (Blattodea: Isoptera) occurring in the state of Paraíba, northeastern Brazil. The genetic data were obtained from 135 COII sequences identified in 28 genera and 48 species. These are the first COII sequences for 15 taxa (31.
View Article and Find Full Text PDFPLoS One
September 2025
Department of Cardiac Surgery, Faculty of Medicine and University Hospital Cologne, University of Cologne, Cologne, Germany.
Background: Cardiac ischemia reperfusion (I/R) injury is a serious consequence of reperfusion therapy for myocardial infarction (MI). Peptidylarginine deiminase 4 (PAD4) is a calcium-dependent enzyme that catalyzes the citrullination of proteins. In previous studies, PAD4 inhibition protected distinct organs from I/R injury by preventing the formation of neutrophil extracellular traps (NETs) and attenuating inflammatory responses.
View Article and Find Full Text PDFJ Agric Food Chem
September 2025
College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
α-Amylase is widely used in various industries. However, current industrial production of α-amylase does not meet the demand, necessitating further enzyme optimization to enhance enzymatic activity. Traditional molecular docking studies have used amylose as a substrate, neglecting the dominant amylopectin structure in natural starch.
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