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Design, synthesis, and evaluation of Bothrops venom serine protease peptidic inhibitors
Silva, Gloria Maria da; Souza, Daniel Henrique Berto de; Waitman, Karoline B; Ebram, Matteo Celano; Fessel, Melissa R; Zainescu, Iuliu Cezar; Portaro, Fernanda C; Heras, Montse; Andrade, Sonia A. de.
  • Silva, Gloria Maria da; Butantan Institute. Laboratory of Pain and Signaling. São Paulo. BR
  • Souza, Daniel Henrique Berto de; Butantan Institute. Laboratory of Pain and Signaling. São Paulo. BR
  • Waitman, Karoline B; Butantan Institute. Laboratory of Pain and Signaling. São Paulo. BR
  • Ebram, Matteo Celano; Butantan Institute. Laboratory of Pain and Signaling. São Paulo. BR
  • Fessel, Melissa R; Butantan Institute. Laboratory of Molecular Biology. São Paulo. BR
  • Zainescu, Iuliu Cezar; University of Oxford. Department of Chemistry. Oxford. GB
  • Portaro, Fernanda C; Butantan Institute. Laboratory of Immunochemistry. São Paulo. BR
  • Heras, Montse; University of Girona. Department of Chemistry. Laboratory of Innovation in Processes and Products of Organic Synthesis. Montilivi Campus. ES
  • Andrade, Sonia A. de; Butantan Institute. Laboratory of Pain and Signaling. São Paulo. BR
J. venom. anim. toxins incl. trop. dis ; 27: e20200066, 2021. graf
Article in English | LILACS, VETINDEX | ID: biblio-1154773
ABSTRACT
In Central and South America, snakebite envenomation is mainly caused by Bothrops spp. snakes, whose venoms feature significant biochemical richness, including serine proteases. The available bothropic antivenoms are efficient in avoiding fatalities, but do not completely neutralize venom serine proteases, which are co-responsible for some disorders observed during envenomation.

Methods:

In order to search for tools to improve the antivenom's, 6-mer peptides were designed based on a specific substrate for Bothrops jararaca venom serine proteases, and then synthesized, with the intention to selectively inhibit these enzymes.

Results:

Using batroxobin as a snake venom serine protease model, two structurally similar inhibitor peptides were identified. When tested on B. jararaca venom, one of the new inhibitors displayed a good potential to inhibit the activity of the venom serine proteases. These inhibitors do not affect human serine proteases as human factor Xa and thrombin, due to their selectivity.

Conclusion:

Our study identified two small peptides able to inhibit bothropic serine proteases, but not human ones, can be used as tools to enhance knowledge of the venom composition and function. Moreover, one promising peptide (pepC) was identified that can be explored in the search for improving Bothrops spp. envenomation treatment.(AU)
Subject(s)


Full text: Available Index: LILACS (Americas) Main subject: Snake Venoms / Antivenins / Bothrops / Serine Proteases Type of study: Prognostic study Limits: Animals Language: English Journal: J. venom. anim. toxins incl. trop. dis Year: 2021 Type: Article Institution/Affiliation country: Butantan Institute/BR / University of Girona/ES / University of Oxford/GB

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Full text: Available Index: LILACS (Americas) Main subject: Snake Venoms / Antivenins / Bothrops / Serine Proteases Type of study: Prognostic study Limits: Animals Language: English Journal: J. venom. anim. toxins incl. trop. dis Year: 2021 Type: Article Institution/Affiliation country: Butantan Institute/BR / University of Girona/ES / University of Oxford/GB