Interrogating the Venom of the Viperid Snake Sistrurus catenatus edwardsii by a Combined Approach of Electrospray and MALDI Mass Spectrometry

dc.creatorChapeaurouge, Alex
dc.creatorReza, Md Abu
dc.creatorMackessy, Stephen P.
dc.creatorCarvalho, Paulo C.
dc.creatorValente, Richard H.
dc.creatorFerreira, André Teixeira
dc.creatorPerales, Jonas
dc.creatorLin, Qingsong
dc.creatorKini, R. Manjunatha
dc.date2015-08-19T13:49:22Z
dc.date2015-08-19T13:49:22Z
dc.date2015
dc.date.accessioned2023-09-26T21:00:30Z
dc.date.available2023-09-26T21:00:30Z
dc.identifierCHAPEAUROUGE, Ana; et al. Interrogating the Venom of the Viperid Snake Sistrurus catenatus edwardsii by a Combined Approach of Electrospray and MALDI Mass Spectrometry. Plos One, v.10, n5, :e0092091, 17p, 2015.
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/11497
dc.identifier10.1371/journal.pone.0092091
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8867633
dc.descriptionThe complete sequence characterization of snake venom proteins by mass spectrometry is rather challenging due to the presence of multiple isoforms from different protein families. In the present study, we investigated the tryptic digest of the venom of the viperid snake Sistrurus catenatus edwardsii by a combined approach of liquid chromatography coupled to either electrospray (online) or MALDI (offline) mass spectrometry. These different ionization techniques proved to be complementary allowing the identification a great variety of isoforms of diverse snake venom protein families, as evidenced by the detection of the corresponding unique peptides. For example, ten out of eleven predicted isoforms of serine proteinases of the venom of S. c. edwardsii were distinguished using this approach. Moreover, snake venom protein families not encountered in a previous transcriptome study of the venom gland of this snake were identified. In essence, our results support the notion that complementary ionization techniques of mass spectrometry allow for the detection of even subtle sequence differences of snake venom proteins, which is fundamental for future structure-function relationship and possible drug design studies.
dc.formatapplication/pdf
dc.languageeng
dc.publisherPlos One
dc.rightsopen access
dc.subjectMALDI Mass Spectrometry
dc.subjectViperid Snake
dc.subjectElectrospray
dc.subjectSistrurus catenatus edwardsii
dc.subjectSerpentes
dc.subjectEspectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
dc.subjectEspectrometria de Massas por Ionização por Electrospray
dc.titleInterrogating the Venom of the Viperid Snake Sistrurus catenatus edwardsii by a Combined Approach of Electrospray and MALDI Mass Spectrometry
dc.typeArticle


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