Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

The effect of neutral salts on protein conformation was first analyzed by Hofmeister in 1888, however, even today this phenomenon is not completely understood. To clarify this effect, we studied changes in the secondary structure of two proteins: human serum albumin with predominantly α-helical structure and porcine pancreas β-trypsin with the typical β-structural arrangement in aqueous solutions of neutral salts (KSCN, KCl, (NH₄)₂SO₄). The changes in the secondary structure were studied at 23 °C and 80 °C by using the second derivative deconvolution method of the IR spectra. Our results demonstrated that the ability of the salts to stabilize/destabilize these two proteins correlates with the Hofmeister series of ions. At the same time, some exceptions were also observed. The destabilization of the native structures of both α-helical albumin and β-structural trypsin upon interaction with neutral salts leads to the formation of intermolecular β-sheets typical for amyloid fibrils or amorphous aggregates. Thus, our quantitative FTIR-spectroscopy analysis allowed us to further clarify the mechanisms and complexity of the neutral salt actions on protein structures which may lead to strategies preventing unwelcome misfolding of proteins.

Optimizing the properties of electrospun polymer-perovskite nanofibers is considered essential for improving the performance of flexible optoelectronic devices. Here, the influence of electrospinning setup parameters (i.e., electrical voltage, collector type (planar or rotary), rotation speed, as well as process time) on the properties (i.e., external structure, perovskite crystallinity, optical properties, thermal properties, the shrinkage ratio, mechanical properties, and long-term stability) of electrospun polyvinylpyrrolidone nanofibers modified with cesium lead iodide nanocrystals has been studied. The results have shown that the structure of nanofibers is related to the electrical voltage, collector rotation speed, and process duration. Perovskite crystallinity and light absorption have improved by increasing the electrical voltage or/and the process time. The polymer’s glass transition temperature is affected by the embedded perovskite and the collector’s rotation speed. The shrinkage ratio and mechanical properties of nanofibers have been controlled by the rotation speed and the electrical voltage. The shrinkage is caused by the stress created in the nanofibers during the electrospinning process. The best mechanical properties can be noticed with the rotary collector at a rotational speed of 500--750 rpm. Nanofibers have shown good long-term stability and high thermal stability. The long-term stability is inversely proportional to the value of the electrical voltage.

In this work, a nanofiber mat based on PHB/PEG with various PEG contents was obtained by electrospinning process. The thermal and mechanical properties of the PHB/PEG nanofiber mat were investigated. In addition, PHB/PEG nanofiber mats were characterized by Fourier transforms infrared spectroscopy (FTIR), differential scanning calorimetry, thermogravimetric analysis, X-ray diffraction, and water contact angle measurement. It was shown that, by increasing the PEG contents from 1 to 4%, the average diameter of PHB nanofibers decreased from 1177 nm to 1101 nm, corresponding to 2% PEG, then the diameter of the fiber increased again from 1101 nm to 1136 nm, corresponding to 4% PEG. Tensile strength increased from 3.6 MPa to 4.4 MPa, then decreased from 4.4 MPa to 2.9 MPa. Thermogravimetric analysis showed a difference in the process of thermal degradation of nanofiber mats. The degree of crystallinity measured by XRD and DSC methods gives different values at some points. The results demonstrated that adding PEG improved the mechanical properties, hydrophobicity, porosity, and thermal stability of the PHB fiber mat, which showed that the PHB/PEG nanofiber mat has great potential for air filtration or water filtration.