Nonlinear Layer-by-Layer Films: Effects of Chain Diffusivity on Film Structure and Swelling

We report on the role of molecular diffusivity in the formation of nonlinearly growing polyelectrolyte multilayers (<i>nl</i>PEMs). Electrostatically bound polyelectrolyte multilayers were assembled from poly­(methacrylic acid) (PMAA) as a polyanion and quaternized poly­(2-(dimethyl­amino)­ethyl methacrylate) (QPC) as a polycation. Film growth as measured by ellipsometry was strongly dependent on the time allowed for each polymer deposition step, suggesting that the diffusivities of the components are crucial in controlling the rate of film growth. Uptake of polyelectrolytes within <i>nl</i>PEMs was relatively slow and occurred on time scales ranging from minutes to hours, depending on the film thickness. Spectroscopic ellipsometry measurements with <i>nl</i>PEM films exposed to aqueous solutions exhibited high (severalfold) degrees of film swelling and different swelling values for films exposed to QPC or PMAA solutions. FTIR spectroscopy showed that the average ionization of film-assembled PMAA increased upon binding of QPC and decreased upon binding of PMAA, in agreement with the charge regulation mechanism for weak polyelectrolytes. The use of neutron reflectometry (NR) enabled quantification of chain intermixing within the film, which was drastically enhanced when longer times were allowed for polyelectrolyte deposition. Diffusion coefficients of the polycation derived from the uptake rates of deuterated chains within hydrogenated films were of the order of 10^–14 cm²/s, i.e., 5–6 orders of magnitude smaller than those found for diffusion of free polymer chains in solution. Exchange of the polymer solutions to buffer inhibited film intermixing. Taken together, these results contribute to understanding the mechanism of the growth of nonlinear polyelectrolyte multilayers and demonstrate the possibility of controlling film intermixing, which is highly desirable for potential future applications

Molecular Weight Dependence of Polymer Chain Mobility within Multilayer Films

Fluorescence recovery after photobleaching has been applied to determine, to our knowledge for the first time, the molecular weight (<i>M</i>_w) dependence of lateral diffusion of polymer chains within layer-by-layer (LbL) films. As shown by neutron reflectometry, polyelectrolyte multilayers containing polymethacrylic acid (PMAA, <i>M</i>_w/<i>M</i>_n < 1.05) of various molecular weights assembled from solutions of low ionic strengths at pH 4.5, where film growth was linear, showed similar diffusion of PMAA in the direction perpendicular to the film surface. At a salt concentration sufficient for unfreezing electrostatically bonded chains, layer intermixing remained almost unaffected (changes <1.0 nm), while the lateral diffusion coefficient (<i>D</i>) scaled with the PMAA molecular weight as <i>D ∼ M</i>_w^–1±0.05

Chain Conformation and Dynamics in Spin-Assisted Weak Polyelectrolyte Multilayers

We report on the effect of the deposition technique on film layering, stability, and chain mobility in weak polyelectrolyte layer-by-layer (LbL) films. Ellipsometry and neutron reflectometry (NR) showed that shear forces arising during spin-assisted assembly lead to smaller amounts of adsorbed polyelectrolytes within LbL films, result in a higher degree of internal film order, and dramatically improve stability of assemblies in salt solutions as compared to dip-assisted LbL assemblies. The underlying flattening of polyelectrolyte chains in spin-assisted LbL films was also revealed as an increase in ionization degree of the assembled weak polyelectrolytes. As demonstrated by fluorescence recovery after photobleaching (FRAP), strong binding between spin-deposited polyelectrolytes results in a significant slowdown of chain diffusion in salt solutions as compared to dip-deposited films. Moreover, salt-induced chain intermixing in the direction perpendicular to the substrate is largely inhibited in spin-deposited films, resulting in only subdiffusional (<2 Å) chain displacements even after 200 h exposure to 1 M NaCl solutions. This persistence of polyelectrolyte layering has important ramifications for multistage drug delivery and optical applications of LbL assemblies

Biocompatible Nanocoatings of Fluorinated Polyphosphazenes through Aqueous Assembly

Nonionic fluorinated polyphosphazenes, such as poly­[bis­(trifluoroethoxy)­phosphazene] (PTFEP), display superb biocompatibility, yet their deposition to surfaces has been limited to solution casting from organic solvents or thermal molding. Herein, hydrophobic coatings of fluorinated polyphosphazenes are demonstrated through controlled deposition of ionic fluorinated polyphosphazenes (iFPs) from aqueous solutions using the layer-by-layer (LbL) technique. Specifically, the assemblies included poly­[(carboxylatophenoxy)­(trifluoroethoxy)­phosphazenes] with varied content of fluorine atoms as iFPs (or poly­[bis­(carboxyphenoxy)­phosphazene] (PCPP) as a control nonfluorinated polyphosphazene) and a variety of polycations. Hydrophobic interactions largely contributed to the formation of LbL films of iFPs with polycations, leading to linear growth and extremely low water uptake. Hydrophobicity-enhanced ionic pairing within iFP/BPEI assemblies gave rise to large-amplitude oscillations in surface wettability as a function of capping layer, which were the largest for the most fluorinated iFP, while control PCPP/polycation systems remained hydrophilic regardless of the film top layer. Neutron reflectometry (NR) studies indicated superior layering and persistence of such layering in salt solution for iFP/BPEI films as compared to control PCPP/polycation systems. Hydrophobicity of iFP-capped LbL coatings could be further enhanced by using a highly porous polyester surgical felt rather than planar substrates for film deposition. Importantly, iFP/polycation coatings displayed biocompatibility which was similar to or superior to that of solution-cast coatings of a clinically validated material (PTFEP), as demonstrated by the hemolysis of the whole blood and protein adsorption studies