Abstract. Hybrid polymeric networks composed of polyacrylamide and chitosan were developed to determine their swelling and ascorbic acid delivery kinetics at various chitosan concentrations. The hybrid acrylamide/chitosan hydrogels were synthesized in aqueous itaconic acid solution (1% w/w). Young's modulus was also evaluated for the hydrogels, and the results were correlated with the swelling properties. Swelling experiments were carried out using three different pH solutions: acidic (pH 4 buffer solution), neutral (distilled water) and basic (pH 10 buffer solution). The results of the swelling study showed that the swelling properties of the network varied with the changes of the pH in the swelling solution, as well as concentration of chitosan. When chitosan concentration increased, the swelling capacity diminished, and therefore Young's modulus increased. The results indicated that the swelling process followed a second order kinetics. The ascorbic acid diffusion inside the hydrogel follows a Fickian mechanism. The ascorbic acid diffusion coefficients are reported as a function of chitosan concentration.
The n-decanephosphonic acid/water and
n-dodecanephosphonic acid/water systems were studied
by
differential scanning calorimetry, hot stage polarized light
microscopy, and FT-IR spectropetry. There is
a rich polymorphism: in both systems there are three liquid
crystalline phases (lamellar Lα and Lβ
and
an inverse cubic phase) plus the isotropic liquid and two solid phases.
One of the solids is an ordinary
cristalline phase and the other is a waxy crystal in which the polar
headgroup network is rigid and ordered
but in which the alkyl chains are partially fluid and disordered.
The water in these systems exists in two
distinct forms: water bound to the headgroups and water which is
effectively free. The polymorphism
of the heptyl and octyl analogues has been studied by Klose et
al.
We have identified a membrane-active region in the HCV NS4B protein by studying membrane rupture induced by a NS4B-derived peptide library on model membranes. This segment corresponds to one of two previously predicted amphipathic helix and define it as a new membrane association domain. We report the binding and interaction with model membranes of a peptide patterned after this segment, peptide NS4B(H2), and show that NS4B(H2) strongly partitions into phospholipid membranes, interacts with them, and is located in a shallow position in the membrane. Furthermore, changes in the primary sequence cause the disruption of the hydrophobicity along the structure and prevent the resulting peptide from interacting with the membrane. Our results suggest that the region where the NS4B(H2) is located might have an essential role in the membrane replication and/or assembly of the viral particle through the modulation of the replication complex. Our findings therefore identify an important region in the HCV NS4B protein which might be implicated in the HCV life cycle and possibly in the formation of the membranous web.
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