Blends of maleated polypropylene and maleated ethylene propylenediene (EPDM-g-MA) were compounded in a twin-screw extruder with a polyetheramine (PEA), polyoxypropylenediamine, as a compatibilizer. The effect of the compatibilizer concentration and molecular weight on the physical properties was investigated. FTIR data showed that the addition of the compatibilizer caused an imide linkage to form between the amine functionality on the PEA and the maleic anhydride (MA) functionality on both the polypropylene (PP) and the rubber backbone. This bond improved the interfacial adhesion between the rubber and the PP matrix, resulting in an improvement in the toughness of the blends. Other improvements in the physical properties of the blends with a compatibilizer compared to the blends without it included notched Izod impact, elongation at yield, and elongation at break. The optimum improvement in properties was found when the level of the compatibilizer was about 3 wt %. These changes in properties correlated well with the morphology observed via optical and scanning electron microscopy.
Amyloid aggregates are found in many neurodegenerative diseases, including Huntington's, Alzheimer's, and prion diseases. The precise role of the aggregates in disease progression has been difficult to elucidate because of the diversity of aggregated states they can adopt. Here, we study the formation of fibrils and oligomers by exon 1 of huntingtin protein. We show that the oligomer states are consistent with polymer micelles that are limited in size by the stretching entropy of the polyglutamine region. The model shows how the sequences flanking the amyloid core modulate aggregation behavior. The N17 region promotes aggregation through weakly attractive interactions, whereas the C38 tail opposes aggregation via steric repulsion. We also show that the energetics of cross-b stacking by polyglutamine would produce fibrils with many alignment defects, but minor perturbations from the flanking sequences are sufficient to reduce the defects to the level observed in experiment. We conclude with a discussion of the implications of this model for other amyloid-forming molecules.
Amyloid aggregates are found in many neurodegenerative diseases including Huntington's, Alzheimer's, and prion diseases. The precise role of the aggregates in disease progression has been difficult to elucidate due to the diversity of aggregated states they can adopt. Here we study the formation of fibrils and oligomers by exon 1 of huntingtin protein. We show that the oligomer states are consistent with polymer micelles that are limited in size by the stretching entropy of the polyglutamine region. The model shows how the sequences flanking the amyloid core modulate aggregation behavior. The N17 region promotes aggregation through weakly attractive interactions, while the C38 tail opposes aggregation via steric repulsion. We also show that the energetics of cross-β stacking by polyglutamine would produce fibrils with many alignment defects, but minor perturbations from the flanking sequences are sufficient to reduce the defects to the level observed in experiment. We conclude with a discussion of the implications of this model for other amyloid forming molecules.
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