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Acinetobacter baumannii is a gram-negative opportunistic bacterium that causes life-threatening infections in immunocompromised hosts. The World Health Organization (WHO) recognizes the high mortality and increasing antimicrobial resistance of A. baumannii and calls for new treatment options.

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In triple-negative breast cancer (TNBC), pro-tumoral macrophages promote metastasis and suppress the immune response. To target these cells, a previously identified CD206 (mannose receptor)-binding peptide, mUNO was engineered to enhance its affinity and proteolytic stability. The new rationally designed peptide, MACTIDE, includes a trypsin inhibitor loop, from the Sunflower Trypsin Inhibitor-I.

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Purpose: Red blood cells (RBCs) senescence and blood rheology during ultra-endurance running events appear to be impacted differently depending on the race distance. The physiological mechanisms underlying these differences are poorly understood.

Methods: We investigated the effects of three different ultra-trail running races performed in La Reunion Island (Mascareignes, "the 70 km", 70 km/4,000 m D+; Trail Du Bourbon, "the 100 km", 100 km/6,090 m D+; Diagonale des Fous, "the 170 km", 170 km/10,500 m D+) on RBC oxidative stress, RBC senescence and blood rheology in 66 finishers (18 "70 km", 24 "100 km", 24 "170 km").

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Purpose: Outer membrane vesicles (OMVs) derived from Gram-negative bacteria naturally serve as a heterologous nano-engineering platform, functioning as effective multi-use nanovesicles for diagnostics, vaccines, and treatments against pathogens. To apply refined OMVs for human theranostic applications, we developed naturally exposed receptor-binding domain (RBD) OMVs grafted with antigen 43 as a minimal modular system targeting angiotensin-converting enzyme 2 (ACE2).

Methods: We constructed -derived OMVs using the antigen 43 autotransporter system to display RBD referred to as viral mimetic Ag43β700_RBD OMVs.

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Improving protein hydrolysis and digestibility in biomass through recombinant peptidases (EC 3.4): Opportunities for monogastric animal diets.

Heliyon

January 2025

CIISA - Centro de Investigação Interdisciplinar em Sanidade Animal, Faculdade de Medicina Veterinária, Universidade de Lisboa, Av. da Universidade Técnica, 1300-477, Lisboa, Portugal.

This study investigates the use of recombinant peptidases (EC 3.4) to improve protein hydrolysis and digestibility in , with a focus on addressing the challenge of reduced protein bioavailability for monogastric animals due to resistant protein-pigment formations, such as phycocyanin, and increased digesta viscosity caused by jellification properties. A library of 192 peptidases was generated, from which 142 soluble peptidases were expressed in and subsequently screened for activity against an suspension .

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