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http://dspace.ucuenca.edu.ec/handle/123456789/37954
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DC Field | Value | Language |
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dc.contributor.author | Camperi, Silvia Andrea | - |
dc.contributor.author | Soares, Andreimar Martins | - |
dc.contributor.author | De Azevedo Calderón, Leonardo | - |
dc.contributor.author | Diniz Sousa, Rafaela | - |
dc.contributor.author | Carvalho Pimenta, Daniel | - |
dc.contributor.author | Azevedo dos Santos, Ana Paula | - |
dc.contributor.author | Benevides Matos, Najla | - |
dc.contributor.author | Da Silva, Saulo Luis | - |
dc.contributor.author | Guerino Stabeli, Rodrigo | - |
dc.contributor.author | Alves da Silva Caldeira, Cleópatra | - |
dc.date.accessioned | 2022-02-04T14:39:01Z | - |
dc.date.available | 2022-02-04T14:39:01Z | - |
dc.date.issued | 2021 | - |
dc.identifier.issn | 0939-4451 | - |
dc.identifier.uri | http://dspace.ucuenca.edu.ec/handle/123456789/37954 | - |
dc.identifier.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85114195344&doi=10.1007%2fs00726-021-03055-y&partnerID=40&md5=91d874f90f1ee8d33a7a3b319c820ca2 | - |
dc.description.abstract | The worrisome emergence of pathogens resistant to conventional drugs has stimulated the search for new classes of antimicrobial and antiparasitic agents from natural sources. Antimicrobial peptides (AMPs), acting through mechanisms that do not rely on the interaction with a specific receptor, provide new possibilities for the development of drugs against resistant organisms. This study sought to purify and proteomically characterize the antimicrobial and antiparasitic peptidomes of B. atrox and B. jararacussu snake venoms against Gram-positive (Staphylococcus aureus, Methicillin-resistant Staphylococcus aureus—MRSA), Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumoniae) bacteria, and the protozoan parasites Leishmania amazonensis and Plasmodium falciparum (clone W2, resistant to chloroquine). To this end, B. atrox and B. jararacussu venom peptides were purified by combination of 3 kDa cut-off Amicon® ultracentrifugal filters and reverse-phase high-performance liquid chromatography, and then identified by electrospray-ionization Ion-Trap/Time-of-Flight mass spectrometry. Fourteen distinct peptides, with masses ranging from 443.17 to 1383.73 Da and primary structure between 3 and 13 amino acid residues, were sequenced. Among them, 13 contained unique sequences, including 4 novel bradykinin-potentiating-like peptides (BPPs), and a snake venom metalloproteinase tripeptide inhibitor (SVMPi). Although commonly found in Viperidae venoms, except for Bax-12, the BPPs and SVMPi here reported had not been described in B. atrox and B. jararacussu venoms. Among the novel peptides, some exhibited bactericidal activity towards P. aeruginosa and S. aureus, had low hemolytic effect, and were devoid of antiparasitic activity. The identified novel antimicrobial peptides may be relevant in the development of new drugs for the management of multidrug-resistant Gram-negative and Gram-positive bacteria | - |
dc.language.iso | es_ES | - |
dc.source | Amino Acids | - |
dc.subject | Snake venom peptidome | - |
dc.subject | Bothrops atrox | - |
dc.subject | Antimicrobial peptide | - |
dc.subject | Peptidomics | - |
dc.subject | Bothrops jararacussu | - |
dc.title | Antimicrobial peptidomes of bothrops atrox and bothrops jararacussu snake venoms | - |
dc.type | ARTÍCULO | - |
dc.ucuenca.idautor | 1757872526 | - |
dc.ucuenca.idautor | 0000-0003-1670-5227 | - |
dc.ucuenca.idautor | 0000-0001-5336-181X | - |
dc.ucuenca.idautor | 0000-0003-2406-0860 | - |
dc.ucuenca.idautor | SGRP-4957-04 | - |
dc.ucuenca.idautor | SGRP-4957-05 | - |
dc.ucuenca.idautor | 0000-0002-0476-920X | - |
dc.ucuenca.idautor | SGRP-4957-08 | - |
dc.ucuenca.idautor | 0000-0003-1032-2188 | - |
dc.ucuenca.idautor | 0000-0003-2669-092X | - |
dc.identifier.doi | 10.1007/s00726-021-03055-y | - |
dc.ucuenca.version | Versión publicada | - |
dc.ucuenca.areaconocimientounescoamplio | 09 - Salud y Bienestar | - |
dc.ucuenca.afiliacion | Camperi, S., University of Buenos Aires, Buenos Aires, Argentina | - |
dc.ucuenca.afiliacion | Guerino, R., Universidade de Sao Paulo - USP, Sao Paulo, Brasil | - |
dc.ucuenca.afiliacion | Alves da Silva, C., Fundacao Universidade Federal de Rondonia (UNIR), Porto Velho, Brasil; Alves da Silva, C., Fundacao Oswaldo Cruz de Rondonia (Fiocruz Rondonia), Porto Velho, Brasil | - |
dc.ucuenca.afiliacion | Diniz, R., Fundacao Oswaldo Cruz de Rondonia (Fiocruz Rondonia), Porto Velho, Brasil; Diniz, R., Fundacao Universidade Federal de Rondonia (UNIR), Porto Velho, Brasil | - |
dc.ucuenca.afiliacion | Da, S., Universidad de Cuenca, Cuenca, Ecuador; Da, S., Universidade do Porto, Porto, Portugal | - |
dc.ucuenca.afiliacion | Azevedo dos, A., Fundacao Universidade Federal de Rondonia (UNIR), Porto Velho, Brasil | - |
dc.ucuenca.afiliacion | De Azevedo, L., Aparício Carvalho University Center (FIMCA), Porto Velho, Brasil | - |
dc.ucuenca.afiliacion | Soares, A., Fundacao Universidade Federal de Rondonia (UNIR), Porto Velho, Brasil; Soares, A., Fundacao Oswaldo Cruz de Rondonia (Fiocruz Rondonia), Porto Velho, Brasil | - |
dc.ucuenca.afiliacion | Carvalho, D., Fundacao Universidade Federal de Rondonia (UNIR), Porto Velho, Brasil | - |
dc.ucuenca.afiliacion | Benevides, N., Fundacao Universidade Federal de Rondonia (UNIR), Porto Velho, Brasil | - |
dc.ucuenca.correspondencia | Alves da Silva Caldeira, Cleópatra, cleobiol@gmail.com | - |
dc.ucuenca.volumen | Volumen 53, número 9 | - |
dc.ucuenca.indicebibliografico | SCOPUS | - |
dc.ucuenca.factorimpacto | 0.89 | - |
dc.ucuenca.cuartil | Q1 | - |
dc.ucuenca.numerocitaciones | 0 | - |
dc.ucuenca.areaconocimientofrascatiamplio | 3. Ciencias Médicas y de la Salud | - |
dc.ucuenca.areaconocimientofrascatiespecifico | 3.2 Medicina Clínica | - |
dc.ucuenca.areaconocimientofrascatidetallado | 3.2.29 Medicina General e Interna | - |
dc.ucuenca.areaconocimientounescoespecifico | 091 - Salud | - |
dc.ucuenca.areaconocimientounescodetallado | 0916 - Farmacia | - |
dc.ucuenca.urifuente | https://link.springer.com/journal/726/volumes-and-issues/53-9 | - |
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documento.pdf | document | 2.05 MB | Adobe PDF | View/Open |
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