In this paper, we present a general, fibril-based structural constitutive theory which accounts for three material aspects of crosslinked filamentous materials: the single fibrillar force response, the fibrillar network model, and the effects of alterations to the fibrillar network. In the case of the single fibrillar response, we develop a formula that covers the entropic and enthalpic deformation regions, and introduce the relaxation phase to explain the observed force decay after crosslink breakage. For the filamentous network model, we characterize the constituent element of the fibrillar network in terms its end-to-end distance vector and its contour length, then decompose the vector orientation into an isotropic random term and a specific alignment, paving the way for an expanded formalism from principal deformation to general 3D deformation; and, more important, we define a critical core quantity over which macroscale mechanical characteristics can be integrated: the ratio of the initial end-to-end distance to the contour length (and its probability function). For network alterations, we quantitatively treat changes in constituent elements and relate these changes to the alteration of network characteristics. Singular in its physical rigor and clarity, this constitutive theory can reproduce and predict a wide range of nonlinear mechanical behavior in materials composed of a crosslinked filamentous network, including: stress relaxation (with dual relaxation coefficients as typically observed in soft tissues); hysteresis with decreasing maximum stress under serial cyclic loading; strain-stiffening under uniaxial tension; the rupture point of the structure as a whole; various effects of biaxial tensile loading; strain-stiffening under simple shearing; the so-called "negative normal stress" phenomenon; and enthalpic elastic behaviors of the constituent element. Applied to compacted collagen gels, the theory demonstrates that collagen fibrils behave as enthalpic elasticas with linear elasticity within the gels, and that the macroscale nonlinearity of the gels originates from the curved fibrillar network. Meanwhile, the underlying factors that determine the mechanical properties of the gels are clarified. Finally, the implications of this study on the enhancement of the mechanical properties of compacted collagen gels and on the cellular mechanics with this model tissue are discussed.
Being an emerging transdermal delivery tool, nanoemulgel, has proved to show surprising upshots for the lipophilic drugs over other formulations. This lipophilic nature of majority of the newer drugs developed in this modern era resulting in poor oral bioavailability, erratic absorption, and pharmacokinetic variations. Therefore, this novel transdermal delivery system has been proved to be advantageous over other oral and topical drug delivery to avoid such disturbances. These nanoemulgels are basically oil-in-water nanoemulsions gelled with the use of some gelling agent in it. This gel phase in the formulation is nongreasy, which favors user compliance and stabilizes the formulation through reduction in surface as well as interfacial tension. Simultaneously, it can be targeted more specifically to the site of action and can avoid first-pass metabolism and relieve the user from gastric/systemic incompatibilities. This brief review is focused on nanoemulgel as a better topical drug delivery system including its components screening, formulation method, and recent pharmacokinetic and pharmacodynamic advancement in research studies carried out by the scientists all over the world. Therefore, at the end of this survey it could be inferred that nanoemulgel can be a better and effective drug delivery tool for the topical system.
Cross-linked soy protein isolate (SPI) gels were produced via single-treatment of SPI with microbial transglutaminase (MTG) for 5 h or 24 h, or with ribose for 2 h, or via combined-treatments of SPI with MTG followed by heating with ribose. Assessment of gel strength and solubility concluded that measures which increased protein cross-links resulted in improved gel strength; however, in most cases the digestibility and amino acid content of the gels were reduced. The combined treated gel of SPI/MTG for 24 h/ribose was more easily digested by digestive enzymes and retained higher amounts of amino acids compared with the control Maillard gels of SPI with ribose. MTG consumed lysine and glutamine and reduced the availability of amino acids for the Maillard reaction with ribose. MTG was able to preserve the nutritional value of SPI against the destructive effect of the Maillard reaction and cross-links.