Profiling of Cyclic Hexadepsipeptides Roseotoxins Synthesized <i>In Vitro</i> and <i>In Vivo</i>: A Combined Tandem Mass Spectrometry and Quantum Chemical Study

Jegorov, Alexandr; Paizs, Béla; Zabka, Martin; Kuzma, Marek; Havlı́ček, Vladimı́r; Giannakopulos, Anastassios E.; Derrick, Peter J.

doi:10.1255/ejms.531

Cited by 35 publications

(24 citation statements)

References 30 publications

(44 reference statements)

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“…Apparently the intense product ion arising from neutral loss of 72 Da is common to all the isaridins (Table S1). To establish that these fragment ions are diagnostic of ␣-hydroxyacid containing cyclodepsipeptides we examined a mixture of roseotoxins [18], produced by Trichothecium roseum. (Table S1).…”

mentioning

confidence: 99%

Identification of α- and β-hydroxy acid containing cyclodepsipeptides in natural peptide mixtures using negative ion mass spectrometry

Thakur

Ranganayaki

Gupta

et al. 2009

J. Am. Soc. Mass Spectrom.

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Natural peptide libraries often contain cyclodepsipeptides containing ␣-or ␤-hydroxy residues. Extracts of fungal hyphae of Isaria yield a microheterogenous cyclodepsipeptide mixture in which two classes of molecules can be identified by mass spectral fragmentation of negative ions. In the case of isaridins, which contain an ␣-hydroxy residue and a ␤-amino acid residue, a characteristic product ion corresponding to a neutral loss of 72 Da is obtained. In addition, neutral loss of water followed by a 72 Da loss is also observed. Two distinct modes of fragmentation rationalize the observed product ion distribution. The neutral loss of 72 Da has also been obtained for a roseotoxin component, which is also an ␣-hydroxy residue containing cyclodepsipeptide. In the case of isariins, which contain a ␤-hydroxy acid residue, ring opening and subsequent loss of the terminal residue as an unsaturated ketene fragment, rationalizes the observed product ion formation. Fragmentation of negative ions provide characteristic neutral losses, which are diagnostic of the presence of ␣-hydroxy or ␤-hydroxy residues. (J Am Soc Mass Spectrom 2009, 20, 2221-2228

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mentioning

confidence: 99%

Identification of α- and β-hydroxy acid containing cyclodepsipeptides in natural peptide mixtures using negative ion mass spectrometry

Thakur

Ranganayaki

Gupta

et al. 2009

J. Am. Soc. Mass Spectrom.

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“…Although sequence determination of linear peptides can be routinely achieved by mass spectrometry [4][5][6], sequencing of cyclic peptides is complicated. There have been reports on sequencing of cyclic peptides by fast atom bombardment (FAB) [7][8][9][10][11][12], Fourier transform ion cyclotron resonance (FTICR) [13], triple quadrupole [14], and ion trap [15][16][17][18] mass spectrometry, and reviews [19,20]. However, studies in most of the reports used known cyclic peptides to develop sequencing methodologies [8-10, 12-15, 17], while only a few publications reported sequencing of unknown cyclic peptides [11,[21][22][23].…”

Section: Introductionmentioning

confidence: 99%

Sequence Elucidation of an Unknown Cyclic Peptide of High Doping Potential by ETD and CID Tandem Mass Spectrometry

Guan

Uboh²,

Soma³

et al. 2011

J. Am. Soc. Mass Spectrom.

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Identification of an unknown substance without any information remains a daunting challenge despite advances in chemistry and mass spectrometry. However, an unknown cyclic peptide in a sample with very limited volume seized at a Pennsylvania racetrack has been successfully identified. The unknown sample was determined by accurate mass measurements to contain a small unknown peptide as the major component. Collision-induced dissociation (CID) of the unknown peptide revealed the presence of Lys (not Gln, by accurate mass), Phe, and Arg residues, and absence of any y-type product ion. The latter, together with the tryptic digestion results of the unusual deamidation and absence of any tryptic cleavage, suggests a cyclic structure for the peptide. Electron-transfer dissociation (ETD) of the unknown peptide indicated the presence of Gln (not Lys, by the unusual deamidation), Phe, and Arg residues and their connectivity. After all the results were pieced together, a cyclic tetrapeptide, cyclo[Arg-Lys-N(C 6 H 9 )Gln-Phe], is proposed for the unknown peptide. Observations of different amino acid residues from CID and ETD experiments for the peptide were interpreted by a fragmentation pathway proposed, as was preferential CID loss of a Lys residue from the peptide. ETD was used for the first time in sequencing of a cyclic peptide; product ions resulting from ETD of the peptide identified were categorized into two types and named pseudo-b and pseudo-z ions that are important for sequencing of cyclic peptides. The ETD product ions were interpreted by fragmentation pathways proposed. Additionally, multi-stage CID mass spectrometry cannot provide complete sequence information for cyclic peptides containing adjacent Arg and Lys residues. The identified cyclic peptide has not been documented in the literature, its pharmacological effects are unknown, but it might be a "designer" drug with athletic performance-enhancing effects.

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“…Going from the gene and proteome levels down to ribosomal and nonribosomal products poses a problem in terms of sample complexity. However, the subtle differences in gene products among genetically similar strains that make their mutual discrimination impossible can be resolved by profiling secondary metabolites (31,32) that are not required for the growth of the fungus but have diverse functions and activities (33).…”

Section: Low-molecular Weight Fungal Molecules Used In Vitro and In Vivomentioning

confidence: 99%

Fungal Metabolites for Microorganism Classification by Mass Spectrometry

Havlı́ček

Lemr

2011

ACS Symposium Series

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Profiling of Cyclic Hexadepsipeptides Roseotoxins Synthesized In Vitro and In Vivo: A Combined Tandem Mass Spectrometry and Quantum Chemical Study

Cited by 35 publications

References 30 publications

Identification of α- and β-hydroxy acid containing cyclodepsipeptides in natural peptide mixtures using negative ion mass spectrometry

Identification of α- and β-hydroxy acid containing cyclodepsipeptides in natural peptide mixtures using negative ion mass spectrometry

Sequence Elucidation of an Unknown Cyclic Peptide of High Doping Potential by ETD and CID Tandem Mass Spectrometry

Fungal Metabolites for Microorganism Classification by Mass Spectrometry

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