Low-protein-fouling poly(ethylene glycol) (PEG-like) plasma polymer films were prepared using radio frequency glow discharge polymerization of diethylene glycol dimethyl ether (DGpp) on top of a heptylamine plasma polymer primer layer. By varying the plasma deposition conditions, the chemistry of the DGpp film was influenced, especially in regard to the level of ether content, which in turn influenced the relative levels of bovine serum albumin and lysozyme protein fouling. Surface potential measurements indicated that these surfaces carried a net negative charge. While protein fouling remained low ( approximately 10 ng/cm2), there was a slightly higher level of the positively charged protein adsorbed on these films than the negative protein. The interaction forces measured between a silica spherical surface on both "high"- and "low"-protein-fouling DGpp films were all repulsive and short ranged (2-3 nm). There was no correlation between the surface forces measured for high- and low-protein-fouling DGpp films. Thus, it appears that enthalpic effects are very important in reducing protein adsorption. We therefore conclude that it is the concentration of residual, ethylene glycol containing species that are the crucial parameter determining protein resistance due to a combination of both entropic and enthalpic effects.

Effects of surface oxidation on the properties of amine plasma polymer (pp) films in aqueous media have not been widely studied, despite their use to control bio‐interfacial properties. Changes in the surface composition of allylamine and heptylamine pp films, on water exposure, were followed by XPS. The surface potential was monitored via AFM measurements and comparison to DLVO theory. Analysis of XPS data implied high initial oxidation rates (rapid quenching of surface radicals). Oxidation of the pp films followed evolution of carbon‐based rather than nitrogen‐based species. Analysis of AFM force data showed changes in the sign of the surface potential with aging from positive to negative. Implications, for example for surface immobilization of molecules in aqueous environments, are also discussed.

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Several growth factors feature prominently in the control of hematopoiesis. Thrombopoietin, a class I hematopoietic cytokine, plays critical roles in regulating hematopoietic stem cell numbers and also stimulates the production and differentiation of megakaryocytes, the bone marrow cells that ultimately produce platelets. Thrombopoietin interacts with the c-Mpl cell-surface receptor. Recently, several peptide and small-molecule agonists and antagonists of c-Mpl have been reported. We conducted a bioinformatics and molecular modeling study aimed at understanding the agonist activities of peptides that bind to c-Mpl, and developed new potent peptide agonists with low nanomolar activity. These agonists also show very high activity in human CD34(+) primary cell cultures, and doubled the mean blood platelet counts when injected into mice.