Potent and broad-spectrum antimicrobial activity of analogs from the scorpion peptide stigmurin

Carmo, Bruno Amorim do; Silva, Alessandra Daniele da; Parente, Adriana Marina e Silva; Furtado, Allanny Alves; Carvalho, Eneas; Oliveira, Johny Wysllas de Freitas; Santos, Elizabeth Cristina Gomes dos; Silva, Marcelo S.; Silva, Sérgio Ruschi Bergamachi; Silva Júnior, Arnóbio Antônio da; Monteiro, Norberto K.; Fernandes-Pedrosa, Matheus F.

Potent and broad-spectrum antimicrobial activity of analogs from the scorpion peptide stigmurin

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dc.contributor.author	Carmo, Bruno Amorim do
dc.contributor.author	Silva, Alessandra Daniele da
dc.contributor.author	Parente, Adriana Marina e Silva
dc.contributor.author	Furtado, Allanny Alves
dc.contributor.author	Carvalho, Eneas
dc.contributor.author	Oliveira, Johny Wysllas de Freitas
dc.contributor.author	Santos, Elizabeth Cristina Gomes dos
dc.contributor.author	Silva, Marcelo S.
dc.contributor.author	Silva, Sérgio Ruschi Bergamachi
dc.contributor.author	Silva Júnior, Arnóbio Antônio da
dc.contributor.author	Monteiro, Norberto K.
dc.contributor.author	Fernandes-Pedrosa, Matheus F.
dc.date.accessioned	2020-07-20T18:34:30Z
dc.date.available	2020-07-20T18:34:30Z
dc.date.issued	2019-01-31
dc.description.resumo	Scorpion venom constitutes a rich source of biologically active compounds with high potential for therapeutic and biotechnological applications that can be used as prototypes for the design of new drugs. The aim of this study was to characterize the structural conformation, evaluate the antimicrobial activity, and gain insight into the possible action mechanism underlying it, for two new analog peptides of the scorpion peptide Stigmurin, named StigA25 and StigA31. The amino acid substitutions in the native sequence for lysine residues resulted in peptides with higher positive net charge and hydrophobicity, with an increase in the theoretical helical content. StigA25 and StigA31 showed the capacity to modify their structural conformation according to the environment, and were stable to pH and temperature variation—results similar to the native peptide. Both analog peptides demonstrated broad-spectrum antimicrobial activity in vitro, showing an effect superior to that of the native peptide, being non-hemolytic at the biologically active concentrations. Therefore, this study demonstrates the therapeutic potential of the analog peptides from Stigmurin and the promising approach of rational drug design based on scorpion venom peptide to obtain new anti-infective agents.	pt_BR
dc.identifier.citation	AMORIM-CARMO, Bruno et al. Potent and broad-spectrum antimicrobial activity of analogs from the scorpion peptide stigmurin. International Journal of Molecular Sciences, [s.l.], v. 20, n. 3, p. 623, jan. 2019. http://dx.doi.org/10.3390/ijms20030623. Disponível em: https://www.mdpi.com/1422-0067/20/3/623. Acesso em: 20 jul. 2020.	pt_BR
dc.identifier.doi	10.3390/ijms20030623
dc.identifier.uri	https://repositorio.ufrn.br/jspui/handle/123456789/29676
dc.language	en	pt_BR
dc.publisher	MDPI	pt_BR
dc.rights	Attribution 3.0 Brazil	*
dc.rights.uri	http://creativecommons.org/licenses/by/3.0/br/	*
dc.subject	Tityus stigmurus	pt_BR
dc.subject	Analog peptides	pt_BR
dc.subject	Scorpion venom	pt_BR
dc.subject	Antimicrobial agent	pt_BR
dc.subject	Molecular dynamics	pt_BR
dc.subject	Bacterial membrane	pt_BR
dc.title	Potent and broad-spectrum antimicrobial activity of analogs from the scorpion peptide stigmurin	pt_BR
dc.type	article	pt_BR