Morais, Ana Heloneida de AraújoOliveira, Gerciane Silva de2022-11-222022-11-222022-08-30OLIVEIRA, Gerciane Silva de. Avaliação da genotoxicidade do inibidor de tripsina isolado de semente de tamarindo (Tamarindus indica L.) e do potencial antibacteriano in vitro e in silico de seus peptídeos derivados. Orientador: Ana Heloneida de Araújo Morais. 2022. 111f. Dissertação (Mestrado em Nutrição) - Centro de Ciências da Saúde, Universidade Federal do Rio Grande do Norte, Natal, 2022.https://repositorio.ufrn.br/handle/123456789/49836Bacterial infections have become a global dimension. As a result, the search for natural and biologically safe therapeutic agents with antibacterial action, such as protease inhibitors, is growing. The genotoxicity of the trypsin inhibitor isolated from tamarind seeds (ITT) was evaluated and the antibacterial effect of its produced peptides was investigated in vitro and in silico. For this, initially, the ITT was obtained by trypsin-Sepharose4B chromatography and identified. Biological safety of 2-dimethyl by blocking ITT cytotoxicity by 3-(4,5- dimethylthiazol-yl)-2,5-tetrazobromide (MTT) method and genotoxicity by micronucleus assay with cytokinesis (CBMN) in CHO-K1 cells, using 0.3 and 0.6 mg/ml. The digestion pattern of the ITT was hydrolysis by means of digestion of the simulated digestion in vitro, simulating the oral protocol, protein and intestinal phases INFOEST, however, digestion fluids were not used for digestion. For determination of digested TT enzyme was monitored/conceivable molecular mass and inhibitory inhibitory activity on trypsin. An in vitro antibacterial activity was tested for the hydrolyzed ITT. For cleavage we used the ITT theoretical, and conformation, 2 2 2Tp 567 theoretical model (being a trip/cleavage number and theoretical model) using a trip number defined by 587, using a determined trip number (analysis determination and model), using the ExPASy server's PeptideCutter parsing tool. Subsequently, to select the peptide with antibacterial potential, these were aligned with the ITTp56/287 to identify the positions of the amino acid residues using the peptide with the highest antibacterial potential that did not follow for the molecular one (DM) using the GROMACS package. ITT (0.0/mL, 0.0/mL) Diurnal cell viability and did not change 0.0 mg, while 0.0 changed in cells, gas and oral intact intestinal enzymes (trypsin and trypsin) were performed TT in cleave the I. The hydrolyzed ITT activity (7mg/mL) evaluated for in vitro antibacterial activity against E. faecalis, S. aureus and S. epidermidis, in bacteriostatic or bactericidal activities. In the silica analysis, Peptidetripchyme59 (TVSQTPIDIPIGLPVR) showed amphipathic amino acid elements, hydrophobicity 0.636 and α-helix structure. In DM, Peptidotrychyme59 showed an interaction potential (EPI) of -518.08 kcal.mol-1 with a Gram-positive bacterial membrane and the threonine and arginine residues showed the best EPI, demonstrating great antimicrobial potential. Therefore, the results bring new perspectives of studies and applications for the ITT and its derived peptides on the antibacterial activity which has great importance in the scientific community, since, for the scientific community to be useful in the development of new therapeutic agents with potential of use to reduce the high mortality rate resulting from microbial infections.Acesso AbertoPeptídeos antimicrobianosInibidor de proteaseSimulação de dinâmica molecularTamarindusmasterThesisCNPQ::CIENCIAS DA SAUDE::NUTRICAO