Pneumolysin/Plasma Protein Adsorption, Bacterial Adherence, and Cell Adhesion Characteristics of a...

This study delivers the first report on a cell-membrane-mimicking polymer system, poly[oxy(4-(13-cholenoatenonyl)-1,2,3-triazoyl-1-methyl)ethylene-random-oxy(4-(13-phosphorylcholinenonyl)-1,2,3-triazoyl-1-methyl)ethylene] (PGA-CholPC) films in various compositions in terms of physicochemical properties, protein adsorptions, bacterial adherences, and human cell adhesions. Higher Chol-containing PGA-CholPC in a self-assembled multi-bilayer membrane structure is confirmed to show excellently high affinity to pneumolysin (a cytolysin) and its C-terminal fragment (domain 4) but substantially suppressed affinity to the N-terminal fragment (domains 1-3) and further to plasma proteins. Furthermore, the adherences of pathogenic bacteria are increased favorably; however, the adhesion and proliferation of a human HEp-2 cell line are hindered severely. In contrast, higher-PC-containing PGA-CholPC membranes promote HEp-2 cell adhesion and proliferation but significantly suppress the adsorptions of pneumolysin and its fragments and plasma proteins as well as bacterial adherence. The results collectively confirm that PGA-CholPC can yield a membrane platform enriched with hydrophobic Chol and hydrophilic and zwitterionic PC moieties in any desired compositions, providing highly selective and sensitive physicochemical characters and biocompatibilities which are demanded for applications in various fields including biomedicine, cosmetics, and environmentally friendly consumer products.