Conformational analysis of protein secondary structure during spray-drying of antibody/mannitol formulations

Effect of drying methods of microencapsulated Lactobacillus acidophilus and Lactococcus lactis ssp. cremoris on secondary protein structure and glass transition temperature as studied by Fourier transform infrared and differential scanning calorimetry

“…These authors stated that the use of sugars, such as sucrose, maltodextrin, or disaccharides, combined with starch maintains the native-like secondary protein components after freeze-drying. In addition, Schüle et al (2007) found that mannitol at relatively low concentration protected antibodies during spraydrying with inlet and outlet temperatures of 90°C and 50°C, which was similar to our spray-drying procedure. Similar results were demonstrated by Tzannis and Prestrelski (1999) and Liao et al (2002) using different sugars as the protein protectant.…”

“…cremoris on secondary protein structure and glass transition temperature as studied by Fourier transform infrared and differential scanning calorimetry 1 stated that certain levels of water activity (a w ) at room temperature contributed to conformational disorder of diphytanoylphosphatidylcholine. Protein conformation was also affected by freeze-and spray-drying (GarzonRodriguez et al, 2004;Schüle et al, 2007); drying process and storage at room temperature at low a w might cause the changes in cell envelopes and secondary structure of proteins of bacteria.…”

Novel dry powder inhalation system based on dispersion of lyophilisates

“…Spray drying is a well-established method in food and pharmaceutical industries with increasing popularity due to its applicability to formulate biopharmaceuticals [50,52]. It is one of the most sophisticated drying techniques and offers many possibilities for modification and particle engineering.…”

A thermodynamic analysis of the binding interaction between polysorbate 20 and 80 with human serum albumins and immunoglobulins: A contribution to understand colloidal protein stabilisation

“…An important aspect to retain the biological activity of proteins is to maintain the protein structure in a specific, three-dimensional conformation [11]. This conformation, which can be investigated using different spectroscopic techniques [12][13][14], is only marginally stable with the free energy for the unfolded to folded, native state ∆G u-f lying between -30 to -80 kJ·mol -1 .…”