Characterisation of the tyrocidine and gramicidin fractions of the tyrothricin complex from Bacillus brevis using liquid chromatography and mass spectrometry

Tang, Xuejun; Thibault, Pierre; Boyd, Robert K.

doi:10.1016/0168-1176(92)87015-7

Cited by 53 publications

(67 citation statements)

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“…Variations are mainly in the variable pentapeptide moiety at the aromatic dipeptide unit containing Trp and/or Phe or at the third variable aromatic residue (generally Tyr) (King & Craig, 1955a, b;Mach & Tatum, 1964;Paladini & Craig, 1954;Ruttenberg & Mach, 1966;Ruttenberg et al, 1965;Tang et al 1992). However, despite the conserved structures of the tyrocidines, it has been found that specific tyrocidines were more active against certain pathogens.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…The more polar Trc B and C ( et al, 2013). Whilst previous results on the major tyrocidines are promising, this clearly accentuated the need to elucidate the conditions that would allow for the maximal production of the different coproduced tyrocidines and analogues described previously by Tang et al (1992).The aim of our study was to elucidate the optimal amino acid supplementation for the manipulation of tyrothricin production by B. aneurinolyticus ATCC 10068 to produce pathogen-specific tailored tyrocidine subsets or to produce extracts that could ease the downstream purification of single peptides. We supplemented culture media with selected amino acids central to the production and variability of the different tyrocidines and analogues.…”

mentioning

confidence: 99%

“…The peptides in the tyrothricin complex, the basic tyrocidines and neutral gramicidins Tang et al 1992) (refer to Table 1), are produced by a series of multi-domain enzymic peptide synthetases that are encoded by the tyrocidine biosynthesis operon (Mootz & Marahiel, 1997) or gramicidin biosynthesis operon, respectively (Kessler et al, 2004). Most of the understanding of the genetic control of tyrocidine production has been garnered from expression systems in B. subtilis (Marahiel et al, 1987;Mootz & Marahiel, 1997), as the tyrocidine producer strain Bacillus aneurinolyticus, previously known as Bacillus brevis (Dubos, 1939), has been found to be genetically less accessible (Marahiel et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

“…Efforts to increase surfactin production have included the alteration of growth medium composition, environmental factors, product removal (Cooper et al, 1981;Ohno et al, 1995;Sheppard & Mulligan, 1987) and the addition of carriers to the growth medium (Drouin & Cooper, 1992;Yeh et al, 2005). Genetic manipulation of B. subtilis has shown some success via the induction of random mutations (Gong et al, 2009;Liu et al, 2006;Mulligan et al, 1989) as well as recombinant technology (Ohno et al, 1992).The peptides in the tyrothricin complex, the basic tyrocidines and neutral gramicidins Tang et al 1992) (refer to et al, 2004). Most of the understanding of the genetic control of tyrocidine production has been garnered from expression systems in B. subtilis (Marahiel et al, 1987;Mootz & Marahiel, 1997), as the tyrocidine producer strain Bacillus aneurinolyticus, previously known as Bacillus brevis (Dubos, 1939), has been found to be genetically less accessible (Marahiel et al, 1987).…”

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confidence: 99%

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Manipulation of the tyrothricin production profile of Bacillus aneurinolyticus

et al. 2013

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A group of non-ribosomally produced antimicrobial peptides, the tyrocidines from the tyrothricin complex, have potential as antimicrobial agents in both medicine and industry. Previous work by our group illustrated that the more polar tyrocidines rich in Trp residues in their structure were more active toward Gram-positive bacteria, while the more non-polar tyrocidines rich in Phe residues had greater activity toward Plasmodium falciparum, one of the major causative pathogens of malaria in humans. Our group also found that the tyrocidines have pronounced antifungal activity, dictated by the primary sequence of the tyrocidine. By simply manipulating the Phe or Trp concentration in the culture medium of the tyrothricin producer, Bacillus aneurinolyticus ATCC 10068, we were able to modulate the production of subsets of tyrocidines, thereby tailoring the tyrothricin complex to target specific pathogens. We optimized the tailored tyrothricin production using a novel, small-scale, high-throughput deep 96-well plate culturing method followed by analyses of the peptide mixtures using ultra-performance liquid chromatography linked to mass spectrometry. We were able to gradually shift the production profile of the tyrocidines and analogues, as well as the gramicidins between two extremes in terms of peptide subsets and peptide hydrophobicity. This study demonstrated that tyrothricin peptide subsets with targeted activity can be efficiently produced by simple manipulation of the aromatic amino acid profile of the culture medium. INTRODUCTIONSince the advent of antimicrobial use, there has been a progressive increase in drug resistance toward conventional antibiotics. This has instigated the search for an alternative class of antimicrobial agents with novel mechanisms of action and rare resistance (Brown & Wright, 2005). Antimicrobial peptides are potential candidates with membrane-linked mechanisms of action as well as possible cellular targets (Brown & Wright, 2005). Their rapid membranolytic activity reduces the likelihood of resistant mutants developing. Furthermore, reduced toxicities of the antimicrobial peptides through greater selectivity toward the more negatively charged bacterial cell membrane allow them to discriminate between pathogen targets and the neutral membranes of plants and animals (Javadpour et al., 1996;Matsuzaki et al., 1991Matsuzaki et al., , 1995Qin et al., 2003). Consequently, antimicrobial peptides show potential in the development of therapeutic agents to treat resistant strains of pathogenic microorganisms or to serve as bio-pesticides and preservatives (Brul & Coote, 1999;Cleveland et al., 2001;Keymanesh et al., 2009).A major limitation to the large-scale use of antimicrobial peptides has been the cost and efficiency of their production (Bradshaw, 2003;Gordon et al., 2005;Marr et al., 2006;Yeaman & Yount, 2003). Automated chemical synthesis to produce antimicrobial peptides remains very costly (Hancock & Lehrer, 1998;Hancock & Sahl, 2006;Marr et al., 2006), while use of transgenic organisms fo...

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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Manipulation of the tyrothricin production profile of Bacillus aneurinolyticus

et al. 2013

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Fragmentation and sequencing of cyclic peptides by matrix-assisted laser desorption/ionization post-source decay mass spectrometry

Schilling

Wang

McMurray

et al. 1999

Rapid Commun. Mass Spectrom.

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A series of synthetic cyclic decapeptides and other smaller cyclic peptides were analyzed using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. The investigated compounds were cyclized in a head-to-tail manner and contained non-proteinaceous amino acids, such as D-phenylalanine, D,L-4-carboxyphenylalanine, epsilon-aminocaproic acid, and gamma-aminobutyric acid, and were synthesized in a program to develop inhibitors of pp60(c-src) (Src), a tyrosine kinase that is involved in signal transduction and growth regulation. Post-source decay (PSD) spectra of the cyclic peptides featured abundant sequence ions. Two preferential ring opening reactions were detected resulting in linear fragment ions with an N-terminus of proline and a C-terminus of glutamic acid, respectively. MALDI-PSD spectra even permitted de novo sequencing of some cyclic peptides. Systematic studies on cyclic peptides using this method of fragmentation have not been reported to date. This work presents an easy mass spectrometric method, MALDI-PSD, for the characterization and identification of cyclic peptides.

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Analysis of Bacitracin B using fast atom bombardment and tandem mass spectrometry

Tetler

Davey

Morris

1993

Biol. Mass Spectrom.

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Bacitracin is a mixture of polypeptide antibiotics produced by the action of Bacillus subtilis and Bacillus licheniformis. The mixture has previously been shown to contain at least ten components, of which only the major component, Bacitracin A, and its oxidized counterpart, Bacitracin F, have been fully structurally evaluated. Using fast atom bombardment ionization with tandem mass spectrometry, three isobaric components of one of the minor constituents of the mixture, Bacitracin B, have been structurally characterized, delineating the three single substitution sites within Bacitracin A where Ile has been replaced by Val.

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Characterisation of the tyrocidine and gramicidin fractions of the tyrothricin complex from Bacillus brevis using liquid chromatography and mass spectrometry

Cited by 53 publications

References 58 publications

Manipulation of the tyrothricin production profile of Bacillus aneurinolyticus

Manipulation of the tyrothricin production profile of Bacillus aneurinolyticus

Fragmentation and sequencing of cyclic peptides by matrix-assisted laser desorption/ionization post-source decay mass spectrometry

Analysis of Bacitracin B using fast atom bombardment and tandem mass spectrometry

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