Ovipin: a chicken eggs antibiotic agent

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 hens 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 chicken egg was subjected the extraction acid, the supernatant was prefractionated in Sep- Pak column and fractionated peptide by reverse-phase high-performance liquid chromatography (RP-HPLC). The antimicrobial activity of the fractions were evaluated through liquid growth inhibition assays. The molecular weight and amino acid sequence was determined by mass spectrometry (MS/MS), the characaterization performed by bioinformatics analysis with Peaks(R) tool and comparision with the NCBI and UniProt-SwisProt database. The physicochemical parameters of the samples were evaluated with online programs. One fraction named Ovipin peptide, showed antimicrobial activity against Gram-positive bacteria (Micrococcus luteus - MIC 1.94 {micro}M) and Filamentous fungus (Aspergillus niger - MIC 31.01 {micro}M). The minimum inhibitory concentration against Cryptococcus neoformans VNI (WM 148) Yeast was 15.51 {micro}M, this microorganism an opportunistic yeast and mainly binds in immunosuppressed or immunocompromissed people. Ovipin is a hydrophoic peptide and not cause significant hemolytic effect against human erythrocytes. 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 an alternative against infections developed by resistant microorganisms, mainly in the fight against Cryptococcus neoformans opportunistic yeast.