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dc.creatorHenrickson, Amy
dc.creatorMontina, Tony
dc.creatorHazendonk, Paul
dc.creatorLomonte, Bruno
dc.creatorNeves Ferreira, Ana Gisele da Costa
dc.creatorDemeler, Borries
dc.date.accessioned2023-08-25T21:02:06Z
dc.date.available2023-08-25T21:02:06Z
dc.date.issued2023
dc.identifier.citationhttps://link.springer.com/article/10.1007/s00249-023-01658-9es_ES
dc.identifier.issn1432-1017
dc.identifier.issn0175-7571
dc.identifier.urihttps://hdl.handle.net/10669/89916
dc.description.abstractWe report the solution behavior, oligomerization state, and structural details of myotoxin-II purified from the venom of Bothrops asper in the presence and absence of sodium dodecyl sulfate (SDS) and multiple lipids, as examined by analytical ultracentrifugation and nuclear magnetic resonance. Molecular functional and structural details of the myotoxic mechanism of group II Lys-49 phospholipase A2 homologues have been only partially elucidated so far, and conflicting observations have been reported in the literature regarding the monomeric vs. oligomeric state of these toxins in solution. We observed the formation of a stable and discrete, hexameric form of myotoxin-II, but only in the presence of small amounts of SDS. In SDS-free medium, myotoxin-II was insensitive to mass action and remained monomeric at all concentrations examined (up to 3 mg/ml, 218.2 μM). At SDS concentrations above the critical micelle concentration, only dimers and trimers were observed, and at intermediate SDS concentrations, aggregates larger than hexamers were observed. We found that the amount of SDS required to form a stable hexamer varies with protein concentration, suggesting the need for a precise stoichiometry of free SDS molecules. The discovery of a stable hexameric species in the presence of a phospholipid mimetic suggests a possible physiological role for this oligomeric form, and may shed light on the poorly understood membrane-disrupting mechanism of this myotoxic protein class.es_ES
dc.language.isoenges_ES
dc.sourceEuropean Biophysics Journal, Núm. 52, pp. 445–457es_ES
dc.subjectMyotoxin IIes_ES
dc.subjectSDSes_ES
dc.subjectanalytical ultracentrifugationes_ES
dc.subjectLys-49es_ES
dc.subjectBothrops asperes_ES
dc.titleSDS‑induced hexameric oligomerization of myotoxin‑II from Bothrops asper assessed by sedimentation velocity and nuclear magnetic resonancees_ES
dc.typeartículo originales_ES
dc.identifier.doi10.1007/s00249-023-01658-9
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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