| Autor: |
Piccinini A; Department of Life and Environmental Sciences, Polytechnic University of Marche, 60131 Ancona, Italy., Lourenço EC; Extremochem, Rua Ivone Silva, 1050-124 Lisboa, Portugal., Ascenso OS; Extremochem, Rua Ivone Silva, 1050-124 Lisboa, Portugal., Ventura MR; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal., Amenitsch H; Institute for Inorganic Chemistry, Graz University of Technology, 8010 Graz, Austria., Moretti P; Department of Life and Environmental Sciences, Polytechnic University of Marche, 60131 Ancona, Italy., Mariani P; Department of Life and Environmental Sciences, Polytechnic University of Marche, 60131 Ancona, Italy., Ortore MG; Department of Life and Environmental Sciences, Polytechnic University of Marche, 60131 Ancona, Italy., Spinozzi F; Department of Life and Environmental Sciences, Polytechnic University of Marche, 60131 Ancona, Italy. |
| Abstrakt: |
Many proteins are usually not stable under different stresses, such as temperature and pH variations, mechanical stresses, high concentrations, and high saline contents, and their transport is always difficult, because they need to be maintained in a cold regime, which is costly and very challenging to achieve in remote areas of the world. For this reason, it is extremely important to find stabilizing agents that are able to preserve and protect proteins against denaturation. In the present work, we investigate, by extensively using synchrotron small-angle X-ray scattering experiments, the stabilization effect of five different sugar-derived compounds developed at ExtremoChem on two model proteins: myoglobin and insulin. The data analysis, based on a novel method that combines structural and thermodynamic features, has provided details about the physical-chemical processes that regulate the stability of these proteins in the presence of stabilizing compounds. The results clearly show that some modified sugars exert a greater stabilizing effect than others, being able to maintain the active forms of proteins at temperatures higher than those in which proteins, in the absence of stabilizers, reach denatured states. |
