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Surfactin
Surfactin is a very powerful surfactant commonly used as an antibiotic. It is a bacterial cyclic lipopeptide, largely prominent for its exceptional surfactant power.〔Mor, A. Peptide-based antibiotics: A potential answer to raging antimicrobial resistance. ''Drug Develop. Res. (2000) 50'': 440–447.〕 Its amphiphilic properties help this substance to survive in both hydrophilic and hydrophobic environments. It is an antibiotic produced by the Gram-positive endospore-forming bacteria ''Bacillus subtilis''.〔Peypoux F, Bonmatin JM, Wallach J. Recent trends in the biochemistry of Surfactin; ''Applied Microbiol Biotechnol. (1999)'' 51:553–63〕 In the course of various studies of its properties, surfactin was found to exhibit effective characteristics like antibacterial, antiviral, antifungal, anti-mycoplasma and hemolytic activities.〔Pooja Singh and Swaranjit Singh Cameotra; Potential applications of microbial surfactants in biomedical sciences; ''Institute of Microbial Technology'', Sector 39 A, Chandigarh 160036, India.〕
==Structure and Synthesis ==
Surfactin's structure consists of a peptide loop of seven amino acids (L-aspartic acid, L-leucine, glutamic acid, L-leucine, L-valine and two D-leucines), and a hydrophobic fatty acid chain thirteen to fifteen carbons long which allows it to penetrate cellular membranes. Glutamic acid and aspartic acid residues at positions 1 and 5 respectively, constituting a minor polar domain. On the opposite side, valine residue at position 4 extends down facing the fatty acid chain, making up a major hydrophobic domain. Below critical micellar concentrations (CMCs) the fatty acid tail can extend freely into solution, and then participate in hydrophobic interactions within micelles.〔Grau, A, J C. Gomez Fernandez, and R Peypoux. A Study on the Interactions of Surfactin With Phospholipid Vesicles. ''BBA (1999)'' 1418: 307–319.〕 This antibiotic is synthesized by a linear nonribosomal peptide synthetase, surfactin synthetase, and has, in solution, a characteristic "horse saddle" conformation that explains its large spectrum of biological activity.〔Nathalie Hue, Laurent Serani, Olivier Laprévote; Structural investigation of cyclic peptidolipids from ''Bacillus subtilis'' by high-energy tandem mass spectrometry; ''Institut de Chimie des Substances Naturelles'', CNRS, avenue de la Terrasse, 91198 Gif-sur-Yvette, France.〕
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