Hydrogels have the ability to retain large amounts of water within their three-dimensional polymer matrices. These attractive materials are used in medicine and the food industry; they can serve as the basis for structured food products, additives, and various ingredients. Gelatin is one of widely used biopolymers to create hydrogels that exhibit biocompatibility and tunable rheological properties. In this study, we offer a comparative analysis of rheological properties of gelatin-based hydrogels (C = 6.67%), including mammalian gelatins from bovine and porcine skins and fish gelatins from commercial samples and samples extracted from Atlantic cod skin. Mammalian gelatins provide high strength and elasticity to hydrogels. Their melting point lies in the range from 22 to 34 °C. Fish gelatin from cod skin also provides a high strength to hydrogels. Commercial fish gelatin forms weak gels exhibiting low viscoelastic properties and strength, as well as low thermal stability with a melting point of 7 °C. Gelatins were characterized basing on the analysis of amino acid composition, molecular weight distribution, and biopolymer secondary structure in gels. Our research provides a unique rheological comparison of mammalian and fish gelatin hydrogels as a tool for the re-evaluation of fish skin gelatin produced through circular processes.

We have studied the molecular properties of water in physically and chemically cross-linked gelatin hydrogels by FTIR-spectroscopy, NMR relaxation, and diffusivity and broadband dielectric spectroscopy, which are sensitive to dynamical properties of water, being a structural marker of polymer network. All experiments demonstrated definite reinforcement of the hydrogel net structure and an increase in the amount of hydrate water. FTIR experiments have shown that the chemical cross-linking of gelatin molecules initiates an increase in the collagen-like triple helices “strength”, as a result of infused restriction on protein molecular mobility. The “strengthening” of protein chains hinders the mobility of protein fragments, introducing complex modifications into the structural properties of water which are remained practically unchanged up to up to 30–40 °C.

Experimental data on the affinity of various substances to albumin are essential for the development of empirical models to predict plasma binding of drug candidates. Binding of 24 substituted benzoic acid anions to bovine serum albumin was studied using spectrofluorimetric titration. The equilibrium constants of binding at 298 K were determined according to 1:1 complex formation model. The relationships between the ligand structure and albumin affinity are analyzed. The binding constant values for m- and p-monosubstituted acids show a good correlation with the Hammett constants of substituents. Two- and three-parameter quantitative structure–activity relationship (QSAR) models with theoretical molecular descriptors are able to satisfactorily describe the obtained values for the whole set of acids. It is shown that the electron-density distribution in the aromatic ring exerts crucial influence on the albumin affinity.

Gelatin, a water-soluble protein, shows unique gellification properties, which determine the active commercial availability of gelatin hydrogels in modern alimentary, cosmetic, and pharmaceutical applications. The traditional sources of gelatin for industrial technologies are pork and bovine skin and bones, which sometimes produce religious and some other restrictions. In recent years, there has been a significant increase in the production of gelatin from alternative sources, such as raw fish materials. Unfortunately, fish gelatin is characterized by weak gelling ability and a decrease in gelation and melting temperature, which are a consequence of the amino acid composition and structural features of fish gelatin. One of the ways to strengthen the natural gelling properties of fish gelatin is the structural modification of gelatin hydrogels by the introduction of polysaccharides of various natural origins. We have studied the association of our laboratory-made fish gelatin with three polysaccharides, namely, κ-carrageenan, alginate, and chitosan, which have distinct chemical structures and gelling capabilities. Structural features of the studied systems were analyzed by small-angle X-ray scattering (SAXS), powder X-ray diffraction (PXRD), and scanning electron microscopy (SEM). We applied computer modeling of molecular interactions between fish gelatin and polysaccharides by means of molecular docking and molecular dynamics approaches. The existence of a correlation between the structure of gelatin-polysaccharide systems and their physicochemical properties was demonstrated by wetting angles (flow angles) and dynamic light scattering (DLS) studies of hydrodynamic sizes and surface ζ-potential.

A dataset containing the experimental values of the equilibrium binding constants of clinical drugs, and some other organic ligands with human and mammalian (predominantly bovine) serum albumins, is assembled. The affinity of drugs to albumin governs their pharmacokinetic properties, related to permeability through physiological barriers and distribution within the organism. The dataset contains 1755 records gathered from 346 original literature sources describing the albumin affinity of 324 different substances. The data were extracted from both articles and existing protein-binding databases applied strict data selection rules in order to exclude the values influenced by the third-party compounds. The dataset provides the details on the experimental conditions of the measurements, such as temperature; protein and ligand concentrations; buffer pH, composition and concentration; and the method and model used for the binding constant calculations. Analysis of the data reveals discrepancies between the values from different studies, as well as the significant influence of the measurement method. Averaging the values from multiple independent measurements from the dataset may help to determine the reliable values of the binding constants. The dataset can be used as the reference dataset for the development of predictive models to calculate binding constants, and as the choice for the experimental setup in the future albumin-binding studies.

Hydrogels based on gelatin–chitosan mixtures have great potential for practical application in the development of new materials in food technology and biomedicine. This study examines the effect of chitosan on the gelling properties, rheological, and structural characteristics of fish gelatin type A hydrogels in the acidic pH range of 3.2–3.9. It was shown that an increase in the chitosan-to-gelatin mass ratio up to 0.15 resulted in a growth in the hydrogel thermal stability and an increase in the elastic modulus, hardness, and yield stress. The structural strength of the fish gelatin–chitosan hydrogel increased due to the strengthening of the binding zones in the fish gelatin gel network in the presence of chitosan. According to scanning electron microscopy, the supramolecular microstructure of the gels demonstrated a significant compaction upon the addition of chitosan to fish gelatin. UV and IR spectroscopy data, as well as changes in zeta potential, showed the formation of supramolecular complexes of fish gelatin with chitosan as a result of hydrophobic interactions between biomacromolecules and the establishment of hydrogen bonds; in this case, electrostatic interactions between macromolecules of fish gelatin and chitosan are practically absent in the acidic pH region. The ability to form supramolecular complexes of different compositions at different mass ratios of polysaccharide-to-fish gelatin makes it possible to obtain hydrogels with high gelling properties, strength, elasticity, and thermal stability comparable to hydrogels of mammalian gelatin.