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Properties of novel surfactin‐derived biosurfactants obtained through solid‐phase synthesis
Author(s) -
Vazquez Leonardo,
Teixeira da Silva Ferreira Andre,
Cavalcante Fernanda Sampaio,
Garcia Israel José P.,
Santos Katia Regietto,
Barbosa Leandro Augusto de Oliveira,
Almeida Marcius da Silva,
Mignaco Julio Alberto,
Fontes Carlos Frederico Leite
Publication year - 2018
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3129
Subject(s) - surfactin , bacillus subtilis , chemistry , combinatorial chemistry , cytotoxicity , heterologous , antimicrobial peptides , peptide , biochemistry , microbiology and biotechnology , bacteria , biology , in vitro , genetics , gene
Eight molecules, four peptides (SPs) and four lipopeptides (LPs) derived by rational design from surfactin, a well‐known secreted biosurfactant from Bacillus subtilis , were produced employing Fmoc‐based solid‐phase synthesis. These new peptides were tested to evaluate their potential biosurfactant and biological activities, aiming at possible applications in industrial, biological, pharmaceutical, and medical use. Five molecules (SP1, SP2, SP4, LP5, and LP8) presented potential for medical uses, mainly due to their drug delivery properties as suggested by their synergistic activity with the antibiotic vancomycin against Staphylococcus aureus . All synthetic peptides showed low toxicity against Vero cell cultures, in assays of hemolysis, and in different cytotoxicity assays. In addition, we found that three peptides (SP1, LP6, and LP7) had potential technological and industrial use because of their emulsifying capacity, low toxicity, and ability to physically stabilize solutions. These novel molecules retained some properties of the parental molecule (surfactin, which was originally obtained through nonribosomal synthesis in Bacillus subtilis ) but have the advantage of being linear peptides, which can be produced at large scales through the use of conventional heterologous protein expression protocols.