AUTOESTRUTURAÇÃO DA TIROSINA EM DIFERENTES SOLVENTES E CONCENTRAÇÕES

Abstract

Recently, researchers have been studying molecular self-assembly, which has attracted attention due to its possibilities of being used in the manufacture of numerous devices. Nanostructures are currently of great interest in the scientific community, mainly because they can be obtained from various materials, increasing the number of possibilities for technological application. Nanotechnology is the application of scientific knowledge based on the manipulation and control of matter to the nana scale, thus making use of size- and structuredependent properties and phenomena different from those associated with individual atoms or molecules. Nanostructures from peptides have been known for a long time and are still of interest to the scientific community, mainly due to the uniformity of self-organization, ease of chemical and physical modification, ability to obtain distinct geometric systems, structural versatility and biocompatibility. This area presents new possibilities for the development of products for daily use, with better performance, reduced production cost and using less raw material. Due to the growing interest of the scientific community, research with new substrates is important because they are relatively cheap, safe, clean and the financial rewards from possible patents are relatively high. In addition to providing the substrate with different functionalities, ensuring improvements in technological advancement. Recently, some works have performed self-structuring from amino acids, but they are still scarce when compared to peptide structures and within the class of peptides, most of the works investigate the peptide diphenylalanine. However, with promising results using Tyrosine, there is an increase in the number of works that lend themselves to understanding the structures based on amino acids. Therefore, the object of this research is to determine if Tyrosine are capable of self-assembly in different solvents and concentrations. To assist in the self-assembly of the structures, the properties of the environment in which the peptide was found were changed, by changing the solvents and the added proportions of solution and solvent. Self-assembly was carried out by mixing an aliquot of solution and another of solvent on a microscope plate, being carried out in two stages, following the principles of the botton-up approach, mounting on a regular surface. The first experiment deals with the self-assembly of tyrosine in different solvents in a 1:1 ratio by volume. The second experiment addresses self-assembly at different concentrations. Afterwards there was the characterization by optical microscopy and the obtained structures were analyzed by ImageJ software. The results ensure that the aromatic nature of Tyrosine acts contributing to the π – π stacking for self-assembly. It is also noted that the conditions of the environment and the physical properties of the solvents directly influence the self-assembly of Tyrosine, in which fibers, gels and tubes are formed.