The intensive and indiscriminate use of antibiotic has increased cases of microorganisms resistance and becoming a worldwide public health problem. In the last years, from natural sources such as hen egg, have received special attention in the discovery of new bioactive compounds. This study aims to identify and characterize a new peptide from chicken egg of Gallus gallus domesticus. The peptide was isolated and purified by high-performance liquid chromatography (HPLC), and its antimicrobial activity was evaluated through liquid growth inhibition assays. The peptide, Ovipin, presented antimicrobial activity against Gram-positive bacteria, Filamentous fungus and Yeast, not cause significant hemolytic effect against human erythrocytes. The molecular weight and amino acid sequence of the peptide was determined by mass spectrometry (MS). Ovipin primary sequence is YVSPVAIVKGLNIPL and a molecular weight of 1,581.94 Da. Ovipin shows 100% and 93.3%, respectively, sequence similarity with the fragments Apolipoprotein B of Gallus gallus and Apolipoprotein B of five others species of Aves. Our data suggest that Ovipin peptide could be a potential therapeutic candidate to be used in combination with other antimicrobial molecules or an alternative led compound for substitution the conventional antibiotics against infections developed by resistant microorganisms.

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