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Type: Artigo de periódico
Title: Koninginins, Phospholipase A2 Inhibitors From Endophytic Fungus Trichoderma Koningii
Author: Souza A.D.L.
Rodrigues-Filho E.
Souza A.Q.L.
Pereira J.O.
Calgarotto A.K.
Maso V.
Marangoni S.
Da Silva S.L.
Abstract: Many isolated compounds from endophytic fungus have been useful to human beings, mainly those with medicinal applications and particularly those that can be used in inflammatory processes. Trichoderma fungi produce substances known as koninginins that have great structural similarity to compounds like flavonoids and vitamin E, which are able to inhibit the phospholipase A2 (PLA2). In this work, koninginins A, E and F (KonA, KonE and KonF, respectivamente) isolated from Trichoderma koningii had their capabilities of inhibiting edema-inducing, myotoxic and enzymatic activities of the total venom of Bothrops jararacussu (jararacuçu) snake analyzed, as well as one of its homolog forms of phospholipases A2 (bjPLA2-group IIB) and human secreted PLA2 protein fusion (hsPLA2-group IIA). KonA was not efficient in inhibiting the three activities analyzed in all the tests performed. Nevertheless, KonE and KonF present great capability in inhibiting the effects provoked not only by the venom but also by both PLA2. The activities inhibition shown by KonE and KonF over the enzymes is significantly higher than those obtained over the total venom. KonE and KonF were slightly more efficient in the inhibition of the group IIB (bjPLA2) PLA2 effects than in the inhibition of the group IIA (hsPLA2) PLA2 effects. KonE and KonF structures are similar to vitamin E and, possibly, the action mode of these molecules is similar to the one produced by the vitamin. These results, apparently, indicate that koninginins E and F, as well as vitamin E, present structural regions that might be used as start points in seeking for new and specific anti-inflammatory drugs against such enzymes. © 2007 Elsevier Ltd. All rights reserved.
Rights: fechado
Identifier DOI: 10.1016/j.toxicon.2007.09.009
Date Issue: 2008
Appears in Collections:Unicamp - Artigos e Outros Documentos

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