dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorMunawar, Aisha
dc.creatorTrusch, Maria
dc.creatorGeorgieva, Dessislava
dc.creatorHildebrand, Diana
dc.creatorKwiatkowski, Marcel
dc.creatorBehnken, Henning
dc.creatorHarder, Soenke
dc.creatorArni, Raghuvir
dc.creatorSpencer, Patrick
dc.creatorSchlueter, Hartmut
dc.creatorBetzel, Christian
dc.date2014-12-03T13:11:08Z
dc.date2016-10-25T20:12:15Z
dc.date2014-12-03T13:11:08Z
dc.date2016-10-25T20:12:15Z
dc.date2014-03-01
dc.date.accessioned2017-04-06T06:26:57Z
dc.date.available2017-04-06T06:26:57Z
dc.identifierToxins. Basel: Mdpi Ag, v. 6, n. 3, p. 850-868, 2014.
dc.identifier2072-6651
dc.identifierhttp://hdl.handle.net/11449/112895
dc.identifierhttp://acervodigital.unesp.br/handle/11449/112895
dc.identifier10.3390/toxins6030850
dc.identifierWOS:000335755700005
dc.identifierWOS000335755700005.pdf
dc.identifierhttp://dx.doi.org/10.3390/toxins6030850
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/923649
dc.descriptionElapid snake venom is a highly valuable, but till now mainly unexplored, source of pharmacologically important peptides. We analyzed the peptide fractions with molecular masses up to 10 kDa of two elapid snake venoms-that of the African cobra, N. m. mossambica (genus Naja), and the Peninsula tiger snake, N. scutatus, from Kangaroo Island (genus Notechis). A combination of chromatographic methods was used to isolate the peptides, which were characterized by combining complimentary mass spectrometric techniques. Comparative analysis of the peptide compositions of two venoms showed specificity at the genus level. Three-finger (3-F) cytotoxins, bradykinin-potentiating peptides (BPPs) and a bradykinin inhibitor were isolated from the Naja venom. 3-F neurotoxins, Kunitz/basic pancreatic trypsin inhibitor (BPTI)-type inhibitors and a natriuretic peptide were identified in the N. venom. The inhibiting activity of the peptides was confirmed in vitro with a selected array of proteases. Cytotoxin 1 (P01467) from the Naja venom might be involved in the disturbance of cellular processes by inhibiting the cell 20S-proteasome. A high degree of similarity between BPPs from elapid and viperid snake venoms was observed, suggesting that these molecules play a key role in snake venoms and also indicating that these peptides were recruited into the snake venom prior to the evolutionary divergence of the snakes.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageeng
dc.publisherMdpi Ag
dc.relationToxins
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectnatriuretic peptides
dc.subjectNotechis scutatus from Kangaroo Island
dc.subjectNaja mossambica mossambica
dc.subjectSnake venom
dc.subjectpharmacologically active peptides
dc.subjectBradykinin potentiating peptides
dc.subjectKunitz-type inhibitor
dc.subjectneurotoxin
dc.subjectcytotoxin
dc.titleElapid Snake Venom Analyses Show the Specificity of the Peptide Composition at the Level of Genera Naja and Notechis
dc.typeOtro


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