Data for: Potential effect of carnosine encapsulated niosomes in age-related protein modifications

Protein modification and alteration are important factors in many age-related diseases such as diabetes and Alzheimer’s disease. Modifications like the formation of advanced glycation end-products (AGE) and advanced oxidation protein products (AOPP) can cause harm to the organism and may contribute...

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description Protein modification and alteration are important factors in many age-related diseases such as diabetes and Alzheimer’s disease. Modifications like the formation of advanced glycation end-products (AGE) and advanced oxidation protein products (AOPP) can cause harm to the organism and may contribute to protein aggregation and amyloid fibrils formation. Carnosine was used as a potential solution for protein modification complications. Furthermore, some organs like the brain are difficult to reach due to the blood-brain barrier. As such, new nano-engineered formulations were sought to bypass unwanted interactions and degradation. Thus, we propose the encapsulation of carnosine in niosomes as a potential solution. Initially, carnosine niosomes were synthesized and characterized. Then, modifications of bovine serum albumin (glycation, oxidation, and aggregation) were induced in vitro where carnosine and carnosine niosomes were added at different concentrations (2.5, 5, and 10mM) to the reactions. In addition, biocomputational and docking studies were performed to elucidate the potential interactions. Data showed a dose-dependent inhibition of AGE, AOPP, and aggregation for both carnosine and niosome carnosine. Furthermore, the results suggest that carnosine interacts with specific amino acids implicated in the protein modification process. Carnosine nano-formulation shows promising potential in age-related protein modification and needs further exploration of its mechanisms.
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Modifications like the formation of advanced glycation end-products (AGE) and advanced oxidation protein products (AOPP) can cause harm to the organism and may contribute to protein aggregation and amyloid fibrils formation. Carnosine was used as a potential solution for protein modification complications. Furthermore, some organs like the brain are difficult to reach due to the blood-brain barrier. As such, new nano-engineered formulations were sought to bypass unwanted interactions and degradation. Thus, we propose the encapsulation of carnosine in niosomes as a potential solution. Initially, carnosine niosomes were synthesized and characterized. Then, modifications of bovine serum albumin (glycation, oxidation, and aggregation) were induced in vitro where carnosine and carnosine niosomes were added at different concentrations (2.5, 5, and 10mM) to the reactions. In addition, biocomputational and docking studies were performed to elucidate the potential interactions. Data showed a dose-dependent inhibition of AGE, AOPP, and aggregation for both carnosine and niosome carnosine. Furthermore, the results suggest that carnosine interacts with specific amino acids implicated in the protein modification process. 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Modifications like the formation of advanced glycation end-products (AGE) and advanced oxidation protein products (AOPP) can cause harm to the organism and may contribute to protein aggregation and amyloid fibrils formation. Carnosine was used as a potential solution for protein modification complications. Furthermore, some organs like the brain are difficult to reach due to the blood-brain barrier. As such, new nano-engineered formulations were sought to bypass unwanted interactions and degradation. Thus, we propose the encapsulation of carnosine in niosomes as a potential solution. Initially, carnosine niosomes were synthesized and characterized. Then, modifications of bovine serum albumin (glycation, oxidation, and aggregation) were induced in vitro where carnosine and carnosine niosomes were added at different concentrations (2.5, 5, and 10mM) to the reactions. In addition, biocomputational and docking studies were performed to elucidate the potential interactions. 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Modifications like the formation of advanced glycation end-products (AGE) and advanced oxidation protein products (AOPP) can cause harm to the organism and may contribute to protein aggregation and amyloid fibrils formation. Carnosine was used as a potential solution for protein modification complications. Furthermore, some organs like the brain are difficult to reach due to the blood-brain barrier. As such, new nano-engineered formulations were sought to bypass unwanted interactions and degradation. Thus, we propose the encapsulation of carnosine in niosomes as a potential solution. Initially, carnosine niosomes were synthesized and characterized. Then, modifications of bovine serum albumin (glycation, oxidation, and aggregation) were induced in vitro where carnosine and carnosine niosomes were added at different concentrations (2.5, 5, and 10mM) to the reactions. In addition, biocomputational and docking studies were performed to elucidate the potential interactions. Data showed a dose-dependent inhibition of AGE, AOPP, and aggregation for both carnosine and niosome carnosine. Furthermore, the results suggest that carnosine interacts with specific amino acids implicated in the protein modification process. Carnosine nano-formulation shows promising potential in age-related protein modification and needs further exploration of its mechanisms.</abstract><pub>Mendeley</pub><doi>10.17632/33bzwshm4j</doi><oa>free_for_read</oa></addata></record>
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Nanoparticles
Protein Aggregation
title Data for: Potential effect of carnosine encapsulated niosomes in age-related protein modifications
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