ResearchPad - Polymers and Plastics Default RSS Feed en-us © 2020 Newgen KnowledgeWorks <![CDATA[Decorin Mimic Regulates Platelet-Derived Growth Factor and Interferon-γ Stimulation of Vascular Smooth Muscle Cells]]>


Following balloon injury, smooth muscle cells (SMCs) serve as targets for many of the pro-inflammatory and pro-fibrotic factors, including platelet-derived growth factor (PDGF) and interferon-γ (IFN-γ) released from activated inflammatory cells and platelets. Previously, our lab designed a mimic of the proteoglycan decorin, termed DS-SILY20, that suppressed vascular SMC proliferation, migration, and protein synthesis in vitro, and injured vessels treated with DS-SILY20 demonstrated reduced hyperplasia in vivo. Here we characterize the effects of DS-SILY20 on modulating PDGF and IFN-γ stimulation in both proliferative and quiescent human SMCs to further evaluate the potential impact of DS-SILY20-SMC interaction on restenosis. Nanomolar dissociation constants were observed between DS-SILY20 and both PDGF and IFN-γ. PDGF significantly increased migration, proliferation, and protein and cytokine expression, as well as increased ERK-1/2 and p38 MAPK phosphorylation in both quiescent and proliferative cultures. However, DS-SILY20 inhibited these increases, presumably through sequestration of the PDGF. Consistent with the complex responses seen with IFN-γ in SMC physiology in the literature, the response of SMC cultures to IFN-γ was variable and complex. However, where increased activity was seen with IFN-γ, DS-SILY20 attenuated this activity. Overall, the results suggest that DS-SILY20 would be an ideal alternative to traditional therapeutics used and may be an effective therapy for the prevention of intimal hyperplasia after balloon angioplasty.

<![CDATA[Direct evidence for grain boundary motion as the dominant restoration mechanism in the steady-state regime of extremely cold-rolled copper]]>

Ultra-fine-grained high-purity copper (99.99%) deformed by means of high-pressure torsion into the steady-state regime was subjected to additional rolling deformation. The microstructural changes as a function of the applied strain were analysed by means of orientation imaging microscopy. It was found that after a distinctive rolling strain a steady state with respect to microstructural features such as grain size, misorientation distribution and texture evolves again. A special spilt specimen technique was used to perform quasi in situ observations of the microstructure between additional strain increments. Profound insights into the local deformation and restoration processes within the steady-state regime were gained. The observations lead to the conclusion that grain boundary migration perpendicular to the rolling direction leads to the disappearance of certain grains, enabling the occurrence of a steady state.

<![CDATA[Structural Properties and Phase Behavior of Crosslinked Networks in Polymer Solutions]]>


Structural properties and phase behavior of crosslinked networks embedded in polymer solutions are theoretically investigated. The partial structure factor of the network is calculated using a matrix formulation of the random phase approximation and the forward scattering limit is correlated with the phase behavior. Swelling and deswelling processes are analyzed in terms of the polymer concentration, the mismatch of solvent quality with respect to polymer and network, the polymers incompatibility and their characteristic sizes. Most studies reported so far in the literature have focussed on the swelling of crosslinked networks and gels in pure solvents but the correlation of the structural properties with the phase behavior in the presence of high molecular weight polymers in solution has not been given sufficient attention. The present work is intended to fill this gap in view of the current efforts to develop novel drug encapsulating and targeted delivery devices.

<![CDATA[Thermodynamic Presynthetic Considerations for Ring-Opening Polymerization]]>


The need for polymers for high-end applications, coupled with the desire to mimic nature’s macromolecular machinery fuels the development of innovative synthetic strategies every year. The recently acquired macromolecular-synthetic tools increase the precision and enable the synthesis of polymers with high control and low dispersity. However, regardless of the specificity, the polymerization behavior is highly dependent on the monomeric structure. This is particularly true for the ring-opening polymerization of lactones, in which the ring size and degree of substitution highly influence the polymer formation properties. In other words, there are two important factors to contemplate when considering the particular polymerization behavior of a specific monomer: catalytic specificity and thermodynamic equilibrium behavior. This perspective focuses on the latter and undertakes a holistic approach among the different lactones with regard to the equilibrium thermodynamic polymerization behavior and its relation to polymer synthesis. This is summarized in a monomeric overview diagram that acts as a presynthetic directional cursor for synthesizing highly specific macromolecules; the means by which monomer equilibrium conversion relates to starting temperature, concentration, ring size, degree of substitution, and its implications for polymerization behavior are discussed. These discussions emphasize the importance of considering not only the catalytic system but also the monomer size and structure relations to thermodynamic equilibrium behavior. The thermodynamic equilibrium behavior relation with a monomer structure offers an additional layer of complexity to our molecular toolbox and, if it is harnessed accordingly, enables a powerful route to both monomer formation and intentional macromolecular design.

<![CDATA[The effect of polymers on the phase behavior of balanced microemulsions: diblock-copolymer and comb-polymers]]>

The effect of some amphipilic diblock-copolymers and comb-polymers on a balanced Winsor III microemulsion system is investigated with the quaternary system n-octyl-β-d-glucoside/1-octanol/n-octane/D2O as basis system. The diblock-copolymers are polyethyleneoxide-co-polydodecenoxide (PEOxPEDODOy) and polyethyleneoxide-co-polybutyleneoxide (PEOxPEBUy), constituted of a straight chain hydrophilic part and a bulky hydrophobic part. Addition of the diblock-copolymer leads to an enhancement of the swelling of the middle phase by uptake of water and oil; a maximum boosting factor of 6 was obtained for PEO111PEDODO25. Nuclear magnetic resonance diffusometry yields the self-diffusion coefficients of all the components in the system. The diffusion experiments provide information on how the microstructure of the bicontinuous microemulsion changes upon addition of the polymers. The reduced self-diffusion coefficients of water and oil are sensitive to the type of polymer that is incorporated in the film. For the diblock-copolymers, as mainly used here, the reduced self-diffusion coefficient of oil and water will respond to how the polymer bends the film. When the film bends away from water, the reduced self-diffusion of the water will increase, whereas the oil diffusion will decrease due to the film acting as a barrier, hindering free diffusion. The self-diffusion coefficient of the polymer and surfactant are similar in magnitude and both decrease slightly with increasing polymer concentration.

<![CDATA[Solid-State NMR Characterization of Autofluorescent Fibrils Formed by the Elastin-Derived Peptide GVGVAGVG]]>


The characterization of the molecular structure and physical properties of self-assembling peptides is an important aspect of optimizing their utility as scaffolds for biomaterials and other applications. Here we report the formation of autofluorescent fibrils by an octapeptide (GVGVAGVG) derived via a single amino acid substitution in one of the hydrophobic repeat elements of human elastin. This is the shortest and most well-defined peptide so far reported to exhibit intrinsic fluorescence in the absence of a discrete fluorophore. Structural characterization by FTIR and solid-state NMR reveals a predominantly β-sheet conformation for the peptide in the fibrils, which are likely assembled in an amyloid-like cross-β structure. Investigation of dynamics and the effects of hydration on the peptide are consistent with a rigid, water excluded structure, which has implications for the likely mechanism of intrinsic fibril fluorescence.