RESUMO
Amyloid aggregation of polypeptides is related to a growing number of pathologic states known as amyloid disorders. At present, it is clear that any proteins submitted to appropriate physicochemical environment can acquire fibrilar conformation. Fourier transform infrared spectroscopy (FTIR) has been a widely used technique to study temperature- induced amyloid-fibrils formation in vitro. In this way, strict changes and temperature controls are required to characterize the physicochemical basis of the amyloid-fibrils formation. In this article, the development of a highly efficient and accurate Peltier-based system to improve FTIR measurements is presented (see An Old Physics Phenomenon Applied to a Serious Biomedical Pathology. The accuracy of the thermostatic control was tested with biophysical parameters on biological samples probing its reproducibility. The design of the present device contributes to maintain the FTIR environment stable, which represents a real contribution to improve the spectral quality and thus, the reliability of the results.