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The relationship between the antimicrobial activity of eugenol and the LPETG peptide structure and associated analysis for docking purposes

Didley Sâmia Paiva Cazelli, Maria Eduarda Sousa Barroso, Rafael Brianti Pizi, Marina Orlandi, Thiago Belarmino de Souza, Diogo Teixeira Carvalho, Arlan da Silva Gonçalves, and Denise Coutinho Endringer

Programa de Pós-Graduação em Ciências Farmacêuticas, Universidade Vila Velha, Vila Velha, Brazil

 

E-mail: endringe@gmail.com

Abstract: Sortase A is responsible for the virulence of Gram-positive pathogens, including staphylococci and streptococci. The LPETG is the peptide surface anchor signal for Sortase A. The inhibitors of this enzyme shared similar binding pattern with substrate LPETG. Eugenol and its derivatives may act as sortase A inhibitor. The antimicrobial activity of eugenol and its derivatives was tested in vitro against bacterial strains: Staphylococcus aureus, Streptococcus mutans and Escherichia coli. All the tested derivatives demonstrated antimicrobial activity. Differences between derivatives in terms of in vitro activity and interactions between the amino acid residues were correlated in the docking analysis for the same derivatives. According to the relationship observed in this study between the antimicrobial activity of eugenol and the LPETG peptide structure, some of the eugenol derivatives proved to be more active inhibiting sortase A than eugenol against microorganisms when tested at the same concentrations.

Keywords: Antimicrobial activity; Eugenol; Synthesized; Structure activity; Docking

Full paper is available at www.springerlink.com.

DOI: 10.1007/s11696-017-0181-0

 

Chemical Papers 71 (10) 1877–1886 (2017)

Thursday, January 23, 2020

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