Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions

• Published in: Molecules (Basel, Switzerland) Vol. 24; no. 11; p. 2077
• Main Authors: Díaz-Roa, Andrea, Espinoza-Culupú, Abraham, Torres-García, Orlando, Borges, Monamaris M, Avino, Ivan N, Alves, Flávio L, Miranda, Antonio, Patarroyo, Manuel A, da Silva, Jr, Pedro I, Bello, Felio J
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 31.05.2019; MDPI
• Subjects: alpha-helix; Antibiotic resistance; Antibiotics; Antiinfectives and antibacterials; Antimicrobial activity; Antimicrobial agents; antimicrobial peptide; Antimicrobial peptides; ATP synthase; Bacteria; Calliphoridae; Deoxyribonucleic acid; DNA; drug; Drug resistance; E coli; Erythrocytes; FLI-1 protein; Fluorescence; Gram-positive bacteria; High-performance liquid chromatography; Liquid chromatography; Mass spectrometry; Mass spectroscopy; Minimum inhibitory concentration; Multidrug resistance; Pathogens; Peptides; Physicochemical properties; Proteins; Pseudomonas aeruginosa; Sarconesiopsis magellanica; Secretions; Staphylococcus infections; Toxicity; Toxicity testing; Colombia; United States > US; alpha-helix; Sarconesiopsis magellanica; antimicrobial peptide; Calliphoridae; drug
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules24112077

Antibiotic resistance is at dangerous levels and increasing worldwide. The search for new antimicrobial drugs to counteract this problem is a priority for health institutions and organizations, both globally and in individual countries. blowfly larval excretions and secretions (ES) are an important source for isolating antimicrobial peptides (AMPs). This study aims to identify and characterize a new AMP. RP-HPLC was used to fractionate ES, using C18 columns, and their antimicrobial activity was evaluated. The peptide sequence of the fraction collected at 43.7 min was determined by mass spectrometry (MS). Fluorescence and electronic microscopy were used to evaluate the mechanism of action. Toxicity was tested on HeLa cells and human erythrocytes; physicochemical properties were evaluated. The molecule in the ES was characterized as sarconesin II and it showed activity against Gram-negative ( MG1655, ATCC 27853, PA14) and Gram-positive ( ATCC 29213, A270) bacteria. The lowest minimum inhibitory concentration obtained was 1.9 μM for A270; the AMP had no toxicity in any cells tested here and its action in bacterial membrane and DNA was confirmed. Sarconesin II was documented as a conserved domain of the ATP synthase protein belonging to the Fli-1 superfamily. The data reported here indicated that peptides could be alternative therapeutic candidates for use in infections against Gram-negative and Gram-positive bacteria and eventually as a new resource of compounds for combating multidrug-resistant bacteria.