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• W3206859553 abstract "Despite advances in the field, hemoincompatibility remains a critical issue for hemodialysis (HD) as interactions between various human blood constituents and the polymeric structure of HD membranes results in complications such as activation of immune system cascades. Adding hydrophilic polymer structures to the membranes is one modification approach that can decrease the extent of protein adsorption. This study conducted molecular dynamics (MD) simulations to understand the interactions between three human serum proteins (fibrinogen [FB], human serum albumin, and transferrin) and common HD membranes in untreated and modified forms. Poly(aryl ether sulfone) (PAES) and cellulose triacetate were used as the common dialyzer polymers, and membrane modifications were performed with 2-hydroxymethyl methacrylate (HEMA) and poly (2-methoxyethyl acrylate) (PMEA), using polydopamine-assisted co-deposition. The MD simulations were used as the framework for binding energy simulations, and molecular docking simulations were also performed to conduct molecular-level investigations between the two modifying polymers (HEMA and PMEA) and FB. Each of the three proteins acted differently with the membranes due to their unique nature and surface chemistry. The simulations show PMEA binds less intensively to FB with a higher number of hydrogen bonds, which reflects PMEA's superior performance compared to HEMA. The simulations suggest PAES membranes could be used in modified forms for blood-contact applications as they reflect the lowest binding energy to blood proteins." @default.
• W3206859553 created "2021-10-25" @default.
• W3206859553 creator A5002765101 @default.
• W3206859553 creator A5058889895 @default.
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• W3206859553 date "2021-10-22" @default.
• W3206859553 modified "2023-09-24" @default.
• W3206859553 title "Effects of mussel‐inspired co‐deposition of 2‐hydroxymethyl methacrylate and poly (2‐methoxyethyl acrylate) on the hydrophilicity and binding tendency of common hemodialysis membranes: Molecular dynamics simulations and molecular docking studies" @default.
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• W3206859553 doi "https://doi.org/10.1002/jcc.26773" @default.
• W3206859553 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34677870" @default.
• W3206859553 hasPublicationYear "2021" @default.
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