Self-Assembly and Its Inhibition in Bolaform Amphiphilic Dendrimers

Self-assembly is scientifically interesting, technologically important, and sometimes life-threatening. A striking example: Alzheimer’s disease is caused by the self-assembly of the â-amyloid fragment of amyloid precursor protein. Such natural amphiphiles normally are very expensive and complicated to isolate. Synthetic mimics that are much cheaper and easier to prepare can facilitate the development of efficient characterization methods, even as they suggest new materials science applications. Two-directional arborols are synthetic bolaform amphiphilic dendrimers. They dissolve in hot water and form reversible gels at room temperature. Bundles of fibrils, which are made by self-assembly of arborols, are found in the gels. The properties of the fibrils are characterized with scattering and microscopy from one hundred micron meters scale to molecular level at nano meter size. The porous nature inside the gels is investigated by comparing the diffusion of fluorescently labeled dextrans in arborol gels with that in water. The time dependence of the self-assembly of two-directional arborols from short fibrils to long ones is tracked by microscopy and light scattering. Addition of a one-directional inhibitor slows the self-assembly. To understand the mechanism, the properties of the one-directional arborols at the air-water interface are addressed. The self-associated arborol fibrils can be disassembled by growing gold nanoparticles in the arborol gels or solutions. In a basic arborol solution or gel, gold nanoparticles with an average diameter below 50 nm are formed after adding a diluted gold ion solution. The arborols act as both reducing agents and stabilizers in the formation of gold nanoparticles. Additionally, the long and thin fibrils in the arborol gel/solution are dismantled. As applications, an attempt to build nano-tunnels in the cross-linked poly(N-isopropyl acrylamide), a temperature sensitive hydrogel, PNIPAM gel, by replacing the preloaded arborol fibrils with water is discussed. Finally, encapsulation of the self-assembly fibrils in giant unilamellar vesicles (GUVs) is tried. As supplemental information, the size variance of liposomes at different lipids/arborols ratios is studied by fluorescence photobleaching recovery (FPR) and light scattering

Microstructure and mineral composition of dystrophic calcification associated with the idiopathic inflammatory myopathies

This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.This work was supported in part by the intramural research programs of NIEHS (FWM, LGR) and NIDCR (PGR), ADAF (NE), NIST (NE, JS), the Medical Research Council, UK (AB through the provision of the facility for the determination of mineralization density at the microscopic scale from BSE imaging) and the Veterinary Advisory Committee of the Horserace Betting Levy Board, UK (AB via support of M Arora)

Enhanced detection of early hepatocellular carcinoma by serum SELDI-TOF proteomic signature combined with alpha-fetoprotein marker.

BACKGROUND: Biomarkers for accurate diagnosis of early hepatocellular carcinoma (HCC) are limited in number and clinical validation. We applied SELDI-TOF-MS ProteinChip technology to identify serum profile for distinguishing HCC and liver cirrhosis (LC) and to compare the accuracy of SELDI-TOF-MS profile and alpha-fetoprotein (AFP) level in HCC diagnosis. PATIENTS AND METHODS: Serum samples were obtained from 120 HCC and 120 LC patients for biomarker discovery and validation studies. ProteinChip technology was employed for generating SELDI-TOF proteomic features and analyzing serum proteins/peptides. RESULTS: A diagnostic model was established by CART algorithm, which is based on 5 proteomic peaks with m/z values at 3324, 3994, 4665, 4795, and 5152. In the training set, the CART algorithm could differentiate HCC from LC subjects with a sensitivity and specificity of 98% and 95%, respectively. The results were assessed in blind validation using separate cohorts of 60 HCC and 60 LC patients, with an accuracy of 83% for HCC and 92% for LC patients. The diagnostic odd ratio (DOR) indicated that SELDI-TOF proteomic signature could achieve better diagnostic performance than serum AFP level at a cutoff of 20 ng/mL (AFP(20)) (92.72 vs 9.11), particularly superior for early-stage HCC (87% vs 54%). Importantly, a combined use of both tests could enhance the detection of HCC (sensitivity, 95%; specificity, 98%; DOR, 931). CONCLUSION: Serum SELDI-TOF proteomic signature, alone or in combination with AFP marker, promises to be a good tool for early diagnosis and/screening of HCC in at-risk population with liver cirrhosis

Improve Dentin Bonding Performance Using a Hydrolytically Stable, Ether-Based Primer

The objective of this study is to replace a traditional methacrylate-based primer (glycine, N-(2-hydroxy-3-(2-methyl-1-oxo-2-propenyl)propyl)-N-(4-methylphenyl) monosodium salt, NTG-GMA) with a hydrolytically stable ether-based primer (glycine, N-2-hydroxy-3-(4-vinylbenzyloxy)-propyl-N-(4-methylphenyl), monosodium salt, NTG-VBGE). The performance and durability of bonding composites to detin of two primers combined with methacrylate-based or ether-based adhesives were evaluated using shear bond strength (SBS) and micro-tensile bond strength (μTBS) combined with thermal cycling. The hydrolysis resistance of NTG-VBGE against hydrolysis was tested by challenging primed hydroxyapatite crystals with an esterase. The hydrophilicity of the primers and the resin spreading kinetics of adhesives on primed dentin were characterized by water contact angle measurements. The new primer NTG-VBGE was found to be compatible with both methacrylate-based adhesives and ether-based adhesives. The highest μTBS values were found in the test group of NTG-VBGE and ether-based adhesive, which was consistent with the resin spreading kinetics results. The more hydrophobic and hydrolytically stable primer/adhesive achieved improved dentin infiltration and bonding strength, suggesting significant potential for further developing dental restorative materials with extended service life

Surface properties of a series of amphiphilic dendrimers with short hydrophobic chains

A series of tree-shaped, amphiphilic dendrimers was synthesized. The products belong to the family of one-directional arborols of the form ([9]-n), where the notation signifies that each molecule has nine hydroxyl groups ([9]-) as the hydrophilic head and an alkyl chain as the hydrophobic moiety (n = 6, 8, or 10 carbon atoms). The surfactant character changes dramatically as the number of methylene groups increases. The critical micelle concentration of [9]-6 was determined, and pressure-area isotherms of the less soluble [9]-8 and [9]-10 were obtained. Large structures existed atop the spread layers. Large structures were also found in solutions of [9]-6