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Starch-derived hydrophilic malto-oligosaccharides (Glc, where n = 1-7) conjugated to hydrophobic solanesol through click chemistry, i.e., Glc-b-Sol copolymers, have demonstrated significant promise in developing fully natural block co-oligomers for solid-state nanopatterning applications.

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Exploiting unique NP1 interface: Oriented immobilization via electrostatic and affinity interactions in a tailored PDA/PEI microenvironment enhanced by concanavalin A.

Talanta

January 2025

College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, No. 30, Puzhu South Road, Nanjing, 211816, China; State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, No. 30, Puzhu South Road, Nanjing, 211816, China. Electronic address:

Enzyme immobilization techniques are crucial for enhancing enzyme stability and catalytic efficiency. Traditional methods such as physical adsorption and simple covalent binding often fail to maintain enzyme activity and stability. In this study, an innovative multi-level immobilization strategy was proposed to achieve efficient targeted immobilization of nuclease P1 (NP1) by fine-tuning the surface microenvironment.

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Background: As cell-free nanotherapeutics, extracellular vesicles derived from mesenchymal stem cells (MSC-EVs) have shown potential therapeutic action against liver diseases. However, their effects on autoimmune hepatitis (AIH) are not yet well understood.

Methods And Results: In this study, we utilized a well-established concanavalin A (Con A)-induced fulminant hepatitis mouse model to investigate the effects of MSC-EVs on AIH.

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The branched structure of amylose was probed using concanavalin A (ConA) lectin, which forms precipitable aggregates with highly branched glucans, such as glycogen and amylopectin. Rice (japonica cultivar) amylose was fractionated from de-fatted, gelatinized starch by precipitation with 1-butanol (BuOH) and purified by ultracentrifugation and repeated crystallization. The purified amylose still has short side chains, whose chain-length (CL) distribution resembles that of amylopectin.

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The complex distribution of functional groups in carbohydrates, coupled with their strong solvation in water, makes them challenging targets for synthetic receptors. Despite extensive research into various molecular frameworks, most synthetic carbohydrate receptors have exhibited low affinities, and their interactions with sugars in aqueous environments remain poorly understood. In this work, we present a simple pyridinium-based hydrogen-bonding receptor derived from a subtle structural modification of a well-known tetralactam macrocycle.

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