Selective Protein Adsorption on Polymer Patterns Formed by Self-Organization and Soft Lithography

• Published in: Biomacromolecules 2009-08, Vol.10 (8), p.2101-2109
• Main Authors: Zemła, Joanna, Lekka, Małgorzata, Raczkowska, Joanna, Bernasik, Andrzej, Rysz, Jakub, Budkowski, Andrzej
• Format: Article
• Language: English
• Subjects: Adsorption; Applied sciences; Cathepsin A - metabolism; Concanavalin A - chemistry; Concanavalin A - metabolism; Exact sciences and technology; Microscopy, Atomic Force; Organic polymers; Physicochemistry of polymers; Plant Lectins - chemistry; Plant Lectins - metabolism; Polymers - chemistry; Polymethyl Methacrylate - chemistry; Properties and characterization; Surface Properties
• ISSN: 1525-7797; 1526-4602
• DOI: 10.1021/bm900598s

Thin films, with both isotropic and ordered patterns of polymer domains, are used as substrates to study selective adsorption of two proteins (concanavalin A and lentil lectin) and to test reconstruction of polymer patterns by these proteins. Integral geometry approach is used to compare quantitatively fluorescence micrographs of protein patches with AFM images of original isotropic patterns, formed during blend casting of polystyrene/poly(methyl methacrylate) and PS/poly(ethylene oxide). Preferential adsorption of both lectins to PMMA phase domains, enhanced for PS/PMMA interfaces is concluded. In turn, protein binding to PS phase regions of PS/PEO blends is highly selective. Ordered protein grouping is obtained as a result of selective adsorption to alternating stripes of polystyrene (partly brominated to enable identification) and cross-linked PEO, prepared with solvent-assisted micromolding applied to PBrS/PEO bilayers. Biological activity test, performed with concanavalin A, confirms preserved functionality of a complementary protein, carboxypeptidase Y, adsorbed to polymer patterns.