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This study describes the isolation of a Lys49 <jats:styled-content style=\"fixed-case\">PLA<\/jats:styled-content><jats:sub>2<\/jats:sub> homologue from <jats:italic>Lachesis muta muta<\/jats:italic> venom using two chromatographic steps: size exclusion and reverse phase. The protein showed a molecular mass of 13,889 Da and was devoid of phospholipase activity on an artificial substrate. The primary structure made it possible to identify an unpublished protein from <jats:italic>L. m. muta<\/jats:italic> venom, named Lmut<jats:styled-content style=\"fixed-case\">TX<\/jats:styled-content>, that presented high identity with other Lys49 <jats:styled-content style=\"fixed-case\">PLA<\/jats:styled-content><jats:sub>2<\/jats:sub>s from bothropic venoms. Synthetic peptides designed from Lmut<jats:styled-content style=\"fixed-case\">TX<\/jats:styled-content> were evaluated for their cytotoxic and antimicrobial activities. Lmut<jats:styled-content style=\"fixed-case\">TX<\/jats:styled-content> was cytotoxic against C2C12 myotubes at concentrations of at least 200 \u03bcg\/mL, whereas the peptides showed a low cytolytic effect. Lmut<jats:styled-content style=\"fixed-case\">TX<\/jats:styled-content> showed antibacterial activity against Gram\u2010positive and Gram\u2010negative bacteria; however, <jats:italic>S. aureus<\/jats:italic><jats:styled-content style=\"fixed-case\">ATCC<\/jats:styled-content> 29213 and <jats:styled-content style=\"fixed-case\">MRSA<\/jats:styled-content> strains were more sensitive to the toxin's action. Synthetic peptides were tested on <jats:italic>S. aureus<\/jats:italic>,<jats:styled-content style=\"fixed-case\"> MRSA<\/jats:styled-content> and <jats:italic>P. aeruginosa<\/jats:italic><jats:styled-content style=\"fixed-case\">ATCC<\/jats:styled-content> 27853 strains, showing promising results. This study describes for the first time the isolation of a Lys49 <jats:styled-content style=\"fixed-case\">PLA<\/jats:styled-content><jats:sub>2<\/jats:sub> from <jats:italic>Lachesis<\/jats:italic> snake venom and shows that peptides from specific regions of the sequence may constitute new sources of molecules with biotechnological potential.<\/jats:p>","DOI":"10.1111\/bcpt.12921","type":"journal-article","created":{"date-parts":[[2017,10,25]],"date-time":"2017-10-25T07:06:45Z","timestamp":1508915205000},"page":"413-423","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Identification of the Molecular Determinants of the Antibacterial Activity of Lmut<scp>TX<\/scp>, a Lys49 Phospholipase A<sub>2<\/sub> Homologue Isolated from <i>Lachesis muta muta<\/i> Snake Venom (Linnaeus, 1766)"],"prefix":"10.1111","volume":"122","author":[{"given":"Rafaela","family":"Diniz\u2010Sousa","sequence":"first","affiliation":[{"name":"Center for the Study of Biomolecules Applied to Heath (CEBio) Oswaldo Cruz Foundation (FIOCRUZ), Fiocruz Rondonia Porto Velho RO Brazil"},{"name":"Medicine Department Federal University of Rondonia (UNIR) Porto Velho RO Brazil"},{"name":"Experimental Biology Posgraduate Program (PGBIOEXP) Federal University of Rondonia (UNIR) Porto Velho RO Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cle\u00f3patra A. 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