Cotton fabric was treated with flame-retardant coatings composed of branched polyethylenimine (BPEI) and sodium montmorillonite (MMT) clay, prepared via layer-by-layer (LbL) assembly. Four coating recipes were created by exposing fabric to aqueous solutions of BPEI (pH 7 or 10) and MMT (0.2 or 1 wt %). BPEI pH 10 produces the thickest films, while 1 wt % MMT gives the highest clay loading. Each coating recipe was evaluated at 5 and 20 bilayers. Thermogravimetric analysis showed that coated fabrics left as much as 13% char after heating to 500 degrees C, nearly 2 orders of magnitude more than uncoated fabric, with less than 4 wt % coming from the coating itself. These coatings also reduced afterglow time in vertical flame tests. Postburn residues of coated fabrics were examined with SEM and revealed that the weave structure and fiber shape in all coated fabrics were preserved. The BPEI pH 7/1 wt % MMT recipe was most effective. Microcombustion calorimeter testing showed that all coated fabrics reduced the total heat release and heat release capacity of the fabric. Fiber count and strength of uncoated and coated fabric are similar. These results demonstrate that LbL assembly is a relatively simple method for imparting flame-retardant behavior to cotton fabric. This work lays the foundation for using these types of thin film assemblies to make a variety of complex substrates (foam, fabrics, etc.) flame resistant.

An intumescent nanocoating composed of poly(allylamine) and poly(sodium phosphate) is deposited layer‐by‐layer on cotton fabric. Fire is extinguished right after ignition on the fabric during vertical flame testing. The individual fibers are conformally coated and bubbles form on the fiber surfaces during burning, which is due to an intumescent effect.

Thin composite films of branched polyethylenimine (BPEI) and Laponite clay platelets were prepared using layer-by-layer assembly. The film thickness was tailored by altering the pH of the aqueous mixtures used to deposit these films, resulting in growth that ranged from 0.5 to 5 nm/bilayer (BL). High-pH BPEI and low-pH clay produced the thickest films. The microstructure of tilted Laponite clay platelet stacks is observed with transmission electron microscopy when using unadjusted BPEI (pH 10.3) and pH 6 Laponite. This recipe resulted in a film with 83 wt % clay and a hardness of 0.5 GPa. In all films, the clay platelets are uniformly deposited and look analogous to a cobblestone path in atomic force microscopy surface images. Several 40-BL films, with thicknesses of 100 nm or more, exhibit reduced moduli ranging from 7 to 10 GPa and hardness of around 0.5 GPa, suggesting that these transparent films could be useful as hard coatings for plastic films. These thin coatings were also deposited onto cotton fabric. Each individual cotton fiber was uniformly coated, and the fabric has significantly more char left after burning than the uncoated fabric. Thermogravimetric analysis results reveal that fabric coated with 10 BLs of BPEI/Laponite produces up to 6 wt % char at 500 degrees C, which is almost 1 order of magnitude greater than that of untreated fabric. This initial study demonstrates that polymer/clay assemblies could improve the thermal stability of cotton and may be useful for fire safety applications.

No abstract

This study was initiated to find small molecule ligands that would induce a functional response when docked with neurotrophin Trk receptors. "Minimalist" mimics of β-turns were designed for this purpose. These mimics are: (i) rigid, yet easily folded into turn-like conformations, and (ii) readily accessible from amino acids bearing most of the natural side chains. Gram quantities of sixteen of these turn mimics were prepared, then assembled into 152 fluorescein-labeled bivalent peptidomimetics via a solution-phase combinatorial method. Fluorescence-based screening of these molecules using cells transfected with the Trk receptors identified 10 potential ligands of TrkC, the receptor for neurotrophin-3 (NT-3). Analogs of these bivalent peptidomimetics with biotin replacing the fluorescein label were then prepared and tested to confirm that binding was not due to the fluorescein. Several assays were conducted to find the mode of action of these biotinylated compounds. Thus, direct binding, survival and neuritogenic, and biochemical signal transduction assays showed 8 of the original 10 hits were agonistic ligands binding to the ectodomain of TrkC. Remarkably, some peptidomimetics afford discrete signals leading to either cell survival or neuritogenic differentiation. The significance of this work is three fold. First, we succeeded in finding small, selective, proteolytically stable ligands for the TrkC receptor; there are very few of these in the literature. Second, we show that it is possible to activate distinct and biased signaling pathways with ligands binding at the ectodomain of wild type receptors. Third, the discovery that some peptidomimetics initiate different modes of cell signaling increases their potential as pharmacological probes and therapeutic leads.The neurotrophins are dimeric protein growth factors that help regulate the peripheral and central nervous systems and other tissues that express the Trk and p75 neurotrophin receptors.(1,2) Trk receptors are relatively selective for, and bind with high affinity (∼K d 10 -11 M) to the neurotrophin. Nerve growth factor (NGF) docks with TrkA, Brain Derived Neurotrophic Factor (BDNF) interacts with TrkB(3), and Neurotrophin-3 (NT-3) interacts preferentially with TrkC but can also bind TrkA and TrkB ( Figure 1a). Ligand binding induces phosphorylation (pTyr) of Trk receptors and associated signaling partners and activation of the neurotrophic biological signals: cell growth, cell survival under stress (trophic activity), and/or cellular differentiation (neuritogenic or neurogenic activity).(4-6) * Correspondence regarding design and synthesis of the peptidomimetics to burgess@mail.tamu.edu, and on the biology and pharmacology to uri.saragovi@mcgill.ca. There is also a second receptor for the neurotrophins, p75, a member of the tumor necrosis factor (TNF) receptor superfamily. All the neurotrophins also bind the p75 receptor, but with lesser affinities (10 -9 to 10 -11 M) than for the Trk receptors. (7-9) The p75 receptor can transduce signals which ...