Chemical Modifications Of Phtx-i Myotoxin From Porthidium Hyoprora Snake Venom: Effects On Structural, Enzymatic, And Pharmacological Properties.

dc.creatorHuancahuire-Vega, Salomón
dc.creatorCorrêa, Daniel H A
dc.creatorHollanda, Luciana M
dc.creatorLancellotti, Marcelo
dc.creatorRamos, Carlos H I
dc.creatorPonce-Soto, Luis Alberto
dc.creatorMarangoni, Sergio
dc.date2013
dc.date2015-11-27T13:31:28Z
dc.date2015-11-27T13:31:28Z
dc.date.accessioned2018-03-29T01:17:22Z
dc.date.available2018-03-29T01:17:22Z
dc.identifierBiomed Research International. v. 2013, p. 103494, 2013.
dc.identifier2314-6141
dc.identifier10.1155/2013/103494
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/23484072
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/200525
dc.identifier23484072
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1300758
dc.descriptionWe recently described the isolation of a basic PLA2 (PhTX-I) from Porthidium hyoprora snake venom. This toxin exhibits high catalytic activity, induces in vivo myotoxicity, moderates footpad edema, and causes in vitro neuromuscular blockade. Here, we describe the chemical modifications of specific amino acid residues (His, Tyr, Lys, and Trp), performed in PhTX-I, to study their effects on the structural, enzymatic, and pharmacological properties of this myotoxin. After chemical treatment, a single His, 4 Tyr, 7 Lys, and one Trp residues were modified. The secondary structure of the protein remained unchanged as measured by circular dichroism; however other results indicated the critical role played by Lys and Tyr residues in myotoxic, neurotoxic activities and mainly in the cytotoxicity displayed by PhTX-I. His residue and therefore catalytic activity of PhTX-I are relevant for edematogenic, neurotoxic, and myotoxic effects, but not for its cytotoxic activity. This dissociation observed between enzymatic activity and some pharmacological effects suggests that other molecular regions distinct from the catalytic site may also play a role in the toxic activities exerted by this myotoxin. Our observations supported the hypothesis that both the catalytic sites as the hypothetical pharmacological sites are relevant to the pharmacological profile of PhTX-I.
dc.description2013
dc.description103494
dc.languageeng
dc.relationBiomed Research International
dc.relationBiomed Res Int
dc.rightsaberto
dc.rights
dc.sourcePubMed
dc.subjectAmino Acids
dc.subjectAnimals
dc.subjectCatalytic Domain
dc.subjectCell Line
dc.subjectGroup Ii Phospholipases A2
dc.subjectMice
dc.subjectNeurotoxins
dc.subjectProtein Structure, Secondary
dc.subjectReptilian Proteins
dc.subjectSnake Venoms
dc.titleChemical Modifications Of Phtx-i Myotoxin From Porthidium Hyoprora Snake Venom: Effects On Structural, Enzymatic, And Pharmacological Properties.
dc.typeArtículos de revistas


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