Structural and functional characterization of a multifunctional alanine-rich peptide analogue from Pleuronectes americanus

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dc.creatorMigliolo, Ludovico
dc.creatorSilva, Osmar Nascimento
dc.creatorSilva, Paula Andreia
dc.creatorReis, Maysa Paula da Costa
dc.creatorCosta, Carolina Rodrigues
dc.creatorSilva, Diego Oliveira Nolasco da
dc.creatorBarbosa, João Alexandre Ribeiro Gonçalves
dc.creatorSilva, Maria do Rosário Rodrigues
dc.creatorBemquerer, Marcelo Porto
dc.creatorLima, Lídia Maria Pinto de
dc.creatorRomanos, Maria Teresa Villela
dc.creatorFreitas, Sonia Maria de
dc.creatorMagalhães, Beatriz Simas
dc.creatorFranco, Octavio Luiz
dc.date.accessioned2019-01-24T11:34:53Z
dc.date.available2019-01-24T11:34:53Z
dc.date.issued2012-10-08
dc.description.abstractRecently, defense peptides that are able to act against several targets have been characterized. The present work focuses on structural and functional evaluation of the peptide analogue Pa-MAP, previously isolated as an antifreeze peptide from Pleuronectes americanus. Pa-MAP showed activities against different targets such as tumoral cells in culture (CACO-2, MCF-7 and HCT-116), bacteria (Escherichia coli ATCC 8739 and Staphylococcus aureus ATCC 25923), viruses (HSV-1 and HSV-2) and fungi (Candida parapsilosis ATCC 22019, Trichophyton mentagrophytes (28d&E) and T. rubrum (327)). This peptide did not show toxicity against mammalian cells such as erythrocytes, Vero and RAW 264.7 cells. Molecular mechanism of action was related to hydrophobic residues, since only the terminal amino group is charged at pH 7 as confirmed by potentiometric titration. In order to shed some light on its structure-function relations, in vitro and in silico assays were carried out using circular dichroism and molecular dynamics. Furthermore, Pa-MAP showed partial unfolding of the peptide changes in a wide pH (3 to 11) and temperature (25 to 95uC) ranges, although it might not reach complete unfolding at 95uC, suggesting a high conformational stability. This peptide also showed a conformational transition with a partial a-helical fold in water and a full a-helical core in SDS and TFE environments. These results were corroborated by spectral data measured at 222 nm and by 50 ns dynamic simulation. In conclusion, data reported here show that Pa-MAP is a potential candidate for drug design against pathogenic microorganisms due to its structural stability and wide activity against a range of targets.pt_BR
dc.identifier.citationMIGLIOLO, Ludovico et al. Structural and functional characterization of a multifunctional alanine-rich peptide analogue from Pleuronectes americanus. Plos One, San Francisco, v. 7, n. 10, e4707, 2012.pt_BR
dc.identifier.doi10.1371/journal.pone.0047047
dc.identifier.issn1932-6203
dc.identifier.issne- 1932-6203
dc.identifier.urihttp://repositorio.bc.ufg.br/handle/ri/16832
dc.language.isoengpt_BR
dc.publisher.countryEstados unidospt_BR
dc.publisher.departmentInstituto de Patologia Tropical e Saúde Pública - IPTSP (RG)pt_BR
dc.rightsAcesso Abertopt_BR
dc.titleStructural and functional characterization of a multifunctional alanine-rich peptide analogue from Pleuronectes americanuspt_BR
dc.typeArtigopt_BR

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