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ISSN 1027-2852 (Electronic)
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2019, Number 2

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Biotecnol Apl 2019; 36 (2)

Methanolic extracts of paratoid gland secretions from Cuban Peltophryne toads contain inhibitory activities against peptidases with biomedical relevance

Pascual-Alonso I, Alonso-Bosch R, Cabrera-Muñoz A, Perera WH, Charli JL

Language: English
References: 41
Page: 2221-2227
PDF size: 566.96 Kb.


ABSTRACT

Peptidases regulate most biochemical and physiological processes and are essential for propagation of infectious agents. Many became established targets for new therapeutic drugs. Amphibian’s skin secretions have evolved as potent defense mechanism against predators and microbials. Although numerous biomedical applications have been documented for this natural source, few examples of peptidase inhibitors have been described. In this contribution we evaluated the inhibitory effect of the methanolic extracts obtained from paratoid gland secretions of four Cuban endemic species of toads (Peltophryne fustiger, P. florentinoi, P. peltocephala and P. taladai) against nine peptidase enzymes from different mechanistic classes. The qualitative chemical analysis of each methanolic extract indicated the presence of triterpenoids and steroids, reducing sugars, phenolic compounds, aminoacids, cardiac glycosides and alkaloids. In all cases, the inhibitory activities vs pAPN, pAPA, and pDPP-IV were dose-dependent; inhibition was reduced at the higher substrate concentration. In addition, P. fustiger secretion dose-dependently inhibited papain, but inhibition was not affected by substrate concentration. We did not detect a dose-dependent inhibition of bovine trypsin and pepsin, and of mPPII, pAPB and pLAP. Additionally, Bufalin inhibited pAPN with an IC50 value of 6.23 ± 0.11 μM and a kinetic behavior indicative of a competitive or non-competitive α >1 mode of inhibition. Thus, extracts from paratoid gland secretions from Cuban toads contain inhibitory activities directed against metallo, serine and cysteine peptidases, whose chemical characterization may generate new lead inhibitors with biomedical relevance. Bufalin emerges as a new classical inhibitor of pAPN, with potential applications in biomedical studies targeting APN.


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