2018
DOI: 10.1016/j.cbi.2017.12.001
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Betulinic, oleanolic and ursolic acids inhibit the enzymatic and biological effects induced by a P-I snake venom metalloproteinase

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Cited by 15 publications
(15 citation statements)
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“…Specifically the metalloproteinase Batx-I from B. atrox venom exhibits weak hemorrhagic activity and lacks coagulant and defibrinating activity, but it is able to induce a mild myonecrosis. This metalloproteinase may contribute to the hemorrhage and local tissue damage observed in patients envenomed by B. atrox from Colombia [32,33], since it constitutes about the 45% of venom proteins. Batx-I hemorrhagic activity is similar to the activity reported for other P-I type SVMPs [34], but with less potency compared to P-III type SVMPs.…”
Section: Inhibition Of Proteolytic Activitymentioning
confidence: 99%
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“…Specifically the metalloproteinase Batx-I from B. atrox venom exhibits weak hemorrhagic activity and lacks coagulant and defibrinating activity, but it is able to induce a mild myonecrosis. This metalloproteinase may contribute to the hemorrhage and local tissue damage observed in patients envenomed by B. atrox from Colombia [32,33], since it constitutes about the 45% of venom proteins. Batx-I hemorrhagic activity is similar to the activity reported for other P-I type SVMPs [34], but with less potency compared to P-III type SVMPs.…”
Section: Inhibition Of Proteolytic Activitymentioning
confidence: 99%
“…Proteolytic activity was assayed on fluorescein conjugates of gelatin using the EnzCheck Gelatinase/Collagenase assay kit (Molecular Probes Inc., Eugene, OR, USA) following the protocol described by [33]. Aliquots of 80 µL of the compounds at different concentrations dissolved in buffer (0.05 M Tris-HCl, 0.15 M NaCl, 5 mM CaCl 2 , 0.2 mM sodium azide) were added to each well of a 96-well plate.…”
Section: Inhibition Of Proteolytic Activitymentioning
confidence: 99%
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“…Different synthetic and natural compounds have demonstrated potential for neutralizing the proteolytic and pharmacological activities of SVMPs, including peptidomimetics Batimastat and Marimastat [ 16 , 17 ], zinc chelating agents such as EDTA, TPEN, DTPA or TTD [ 17 , 18 ], synthetic compounds, such as quinolinones [ 19 ] or thiosemicarbazones [ 20 ], and plant derived inhibitors, such as phenolic compounds [ 21 , 22 ], diterpenoids [ 23 ] and triterpenic acids [ 24 ]. In addition, computational approaches, such as molecular docking and molecular dynamics simulations have been used to study the interaction mechanisms of SVMP inhibitors and to identify new candidate compounds which were subsequently verified in experiments [ 20 , 25 , 26 , 27 ].…”
Section: Introductionmentioning
confidence: 99%
“…Thus, in this work, we use the ABF method and an approach similar to funnel metadynamics to compute the standard binding free energies and analyze the atomic interactions that give rise to the binding of betulinic, ursolic, oleanolic, -boswellic and madecassic acids, as well as betulin ( Figure 2 ), to the active site of the metalloproteinase BaP1. Some of these compounds were previously reported as inhibitors of the lethal, proteolytic and hemorrhagic activity of whole snake venoms and isolated metalloproteinases [ 24 , 41 ]. The computational results obtained through the ABF method are compared with experimental data of inhibition of the proteolytic activity of Batx-I.…”
Section: Introductionmentioning
confidence: 99%